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STATE UNIVERSITY OF MEDICINE AND PHARMACY“NICOLAE TESTEMIŢANU”

Gavriliuc Ludmila

BIOCHEMISTRYTests for students

(Methodic material)

CHIŞINĂU2010

STATE UNIVERSITY OF MEDICINE AND PHARMACY“NICOLAE TESTEMIŢANU”

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Gavriliuc Ludmila

BIOCHEMISTRYTests for students(Methodic material)

ChişinăuEditorial-Poligraphic Center Medicine

2010

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CZU 577.1 (079) G26

Aprobat de Consiliul metodic central cu nr.1 din 11.02.2010

Autor: Gavriliuc Ludmila – profesor universitar, doctor habilitatîn medicină

Recenzenţi: VovcVictor – profesor universitar, doctor habilitat in medicina, sef catedrei Fiziologie omului

Cemortan Igor – conferentiar, doctor in biologie, sef catedrei Biologie moleculara si Genetica umana

Panciuc Liliana - lector universitar catedrei Limbi moderneCostin Rodica – lector superior universitar catedrei Limbi moderne

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CONTENTS

IntroductionProgramTest I. 1. Amino acids. Chemical structure of proteins. Enzy-

mes.2. Nucleic acids. Protein synthesis.3. Metabolism. Biological oxidation. Respyratory chain.4. Carbohydrates: chemical structure and metabolism.

Test II. 1. Lipids: chemical structure and metabolism.2. Catabolism of simple proteins. Metabolism of nuc-

leoproteins and hemoproteins.3. Hormones: chemical structure, mechanism action,

metabolic role.4. Blood: metabolism of blood cells, chemical com-

position of blood plasma and their metabolic role.Buffer systems of blood. Hemostasis.

Biochemical indices (parameters)Bibliography (Literature)

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INTRODUCTION

Medical education worldwide is undergoing major change. Anintegrated approach to teaching and learning has resulted in ablurring of the distinctions between the individual basic medicalsciences and the clinical specialities. Integration of pathology, in-cluding clinical chemistry, with other clinical specialities, shouldemphasize its relevance and importance to clinical practice.

This book includes the Program, Tests and Biochemical indi-ces (parameters) of the blood serum, urine and saliva.

These tests are based on materials in Biochemistry and Clini-cal Biochemistry (also known as Clinical Chemistry or ChemicalPathology) according to the Program and not as an isolated specia-lity and in a context in which it is used clinically. The centralfunction of Chemical Pathology or Clinical Chemistry laboratoryis to provide biochemical information for the management of pa-tients. Such information will be of value only if it is accurate andrelevant, and if its significance is appreciated by the clinician sothat it can be used appropriately to guide clinical decision-making.Biochemical tests are used extensively in medicine, both in rela-tion to diseases that have an obvious metabolic basis (diabetesmellitus, hypothyroidism) and those in which biochemical changesare a consequence of the disease (renal failure, malabsorption).Biochemical tests are used in diagnosis, prognosis, monitoring andscreening.

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PROGRAM OF BIOCHEMISTRY SUBJECT

INTRODUCTIONSubject of Biochemistry. Biochemistry importance for medici-

ne. The greatest discoveries in Biochemistry in the XXth century.Peculiarities of the alive matter, levels and methods of its study.

Chapter I

PROTEIN STRUCTURE

Amino acids: classes, structure, amphoteric and electro-che-mical properties. Utility of amino acids in pharmacy and therapy.Peptides and proteins, protein’s classifications. Simple and conju-gated proteins, brief characteristics. Peptide bond, genetic changesof the amino acids sequence, hereditary proteinopathies (moleculardiseases). Levels of proteins organization: primary, secondary,tertiary, quaternary structures and domains. Analysis of proteinconformation: Sanger's, Edman's methods, sequencing of peptidefragments, X-ray crystallography, ultraviolet light spectroscopy,nuclear magnetic resonance. Properties of proteins: molecularmass, thermolability, solubility, amphoteric and charge. Structure-function relationships in proteins, selective interaction with ligands,ligand’s recognition. Simple proteins: histones, albumins, globu-lins, their functions and physico-chemical characteristics. Conjuga-ted (complex) proteins: nucleo-, chromo-, phospho-, glyco-, metallo-,lipoproteins (brief characteristics). Hemoglobin, collagen, immu-noglobulins, Ca2+-binding proteins: peculiarities of structure andfunction. Peculiarities of amino acid composition in collagen,structure, properties and types of collagens. Proteins solutions:types, properties and peculiarities. The purification and analysis ofproteins: salting, dialysis, ultracentrifugation, chromatography,electrophoresis.

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Chapter II

ENZYMES

Biological role of enzymes. Common properties and differren-ces from chemical catalysts. Structure of active center, role in thecatalytic act. Allosteric site: structure, role, modulators. Chemicalnature of enzymes: simple and conjugated proteins. Cofactors,coenzymes and prosthetic groups. The role of water–soluble vita-mins as coenzymes (B1, B2, B6, B12, PP, folic acid, pantothenicacid, biotin, vit. C). Utility of provitamins and vitamins in therapy.

Mechanism of enzyme catalysis. Regulation of enzymes: acti-vation (partial proteolysis, addition of cofactor, covalent modifica-tion, allosteric, quaternary autoassembling) and inhibition: compe-titive (isosteric), noncompetitive, uncompetitive, allosteric, pro-duct inhibition (retroinhibition). Utility in medicine of competitivedrugs (sulphanilamides, F-uracil, etc.).

Enzyme's properties: thermolability, pH influence, specificity(lock and key and induced-fit theories). Types of enzyme specificity.

Genetic diversity of the enzymes: isoenzymes (LDH, CPK).Proenzymes. Organization of multienzymic systems. Compartmen-talization.

Enzyme nomenclature. Measurement and measures of enzy-mes activity. Methods of enzymes separation and purification.Affinity chromatography.

Usage of enzymes assay in diagnostics. Enzymes as drugs.Immobilized enzymes. The use of immobilized enzymes in the the-nological syntheses of a number of hormonal preparations asdrugs, and in high-sensitive analyses of drugs.

Chapter III

NUCLEIC ACIDS

Structural components of the nucleic acids: nitrogenous bases,pentose sugar, phosphate group, their structure, properties.

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Nucleosides and nucleotides: structure, nomenclature, role.Cyclic nucleotides: cAMP (3’,5’cAMP) and cGMP (3’,5’cGMP).

Types of the nucleic acids: DNA, RNA, their distribution inthe cell and biological role.

Nucleic acids structure. DNA structures: primary, secondary,tertiary, nucleosomes, and chromatin. RNA structures: primary, se-condary and tertiary. Structure of tRNA. General aspects ofmRNA and rRNA structure.

Replication (synthesis of DNA): necessary compounds, themultienzymic system, stages, DNA repair.

Transcription: necessary compounds, the multienzymic sys-tem, stages. Post-transcription modification of mRNA. Reversetranscription.

The genetic code and its properties. Mutations and mutagens.Genetic diseases. Inhibitors of proteins synthesis at different levels.Genetic engineering, its means for biopharmacy and medicine.

Translation (protein synthesis). Activation of the amino acids:stages, enzymes, energy. Stages and mechanism of polypeptidechain synthesis. Post-translational modification of the proteins. Pe-culiarities of collagen and immunoglobulins biosynthesis. Proteinfolding. Control of protein synthesis in prokaryotes and eukariotes.Usage of the drugs as inhibitors of replication, transcription andtranslation in medicine.

Chapter IV

INTRODUCTION TO METABOLISM

Metabolism, its stages: anabolism and catabolism. Stages ofcatabolism: final common pathway, its importance.

Bioenergetics: thermodynamic concepts, enthalpy, entropy,free energy, the standard state of the cell. Dehydrogenation: themain energy sources in the human organism.

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High-energy phosphate compounds. ATP: chemical structure,importance, ATP-ADP cycle. Mechanisms of ATP biosynthesis innature: oxidative phosphorylation, substrate phosphorylation, pho-tophosphorylation (photosynthesis).

The mitochondria structure. Oxidative decarboxilation of piru-vate to acetyl-SCoA: multi enzymic complex, reactions, products,its regulation and interrelation with the Krebs cycle.

The tricarboxylic acid cycle (TAC, Krebs cycle): reactions,enzymes, coenzymes, products, regulation, anaplerotic reactions,interrelation with Respiratory Chain.

Mitochondrial electron transport chain (Respiratory Chain), itstypes. Organization of the electron transport chain. Oxidation–reduction (redox) potential and mechanism of ATP production.ATP formation sites, phosphorylation points. A coupling ofrespiration with phosphorylation: oxydative phosphorylation, theP/O ratio. Chemiosmotic or proton-driving hypothesis Mitchell.Uncouples of oxidative phosphorylation. Agents affecting energymetabolism in cells (hormones, drugs, toxins).

Microsomal oxidation: microsomal electron transport chains(NAD-dependent and NADP-dependent chains), their organiza-tion. Role of cytochrome P450. Radical species of oxygen and lipidperoxidation. Protective antioxidative systems: enzymic and nonen-zymic. Vitamins- antioxidants as drugs and their use in medicine.

Chapter V

CARBOHYDRATE CHEMISTRY AND METABOLISM

Definition, classifications, nomenclature and chemical structu-re of carbohydrates. Properties of the most important monosaccha-rides, disaccharides, polysaccharides and carbohydrate derivatives.

Digestion and absorption of carbohydrates (sugars) intogastro-intestinal tract.

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Glycogen metabolism: reactions, enzymes, neuro-hormonalregulation of glycogen biosynthesis and glycogenolysis. Geneticdefects in glycogen metabolism (Von Gierke, Pompe, Forbes di-seases, etc.).

Glycolysis: stages, reactions, enzymes and coenzymes, enzy-mic control of glycolysis. Anaerobic glycolysis: production ATPas substrate phosphorylation. Aerobic glycolysis (aerobic oxida-tion of glucose): high-energy phosphate (ATP) production, role ofa-glycerophosphate and malate-aspartate shuttle mechanisms.Energy balance of glucose oxidation (to CO2 and H2O).

Gluconeogenesis: the gluconeogenic pathway, energetics andsubstrates for gluconeogenesis. The Cory and alanine cycles. Hor-monal control of gluconeogenesis and its pathology.

Pentose phosphate (apotomic) pathway or shunt: functionalsignificance, chemical reactions for pentoses production, regula-tion and biorole.

Metabolism of fructose, galactose and lactose: pathways, sig-nificance and hereditary defects. Biosynthesis of lactose: pathway,control and functional significance. Glucuronic acid cycle: signifi-cance, pathway. Alcohol fermentation: reactions, energetic output,significance.

Regulation of carbohydrate metabolism: metabolic and hor-monal control of the blood serum glucose concentration in healthyand in patients. Diabetes mellitus: metabolic disturbances, mecha-nism hyperglycemia, glucosuria, ketonemia, ketonuria, diabetic co-ma. Drugs used for correction of diabetes mellitus.

Chapter VI

LIPID CHEMISTRY AND METABOLISM

Nature, functions, classifications, structure and properties offatty acids, acylglycerols, phosphoglycerides, sphingomyelin, sphin-golipids, cholesterol and its esters. Fat-soluble vitamins (A, E, D, K):

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structure, biorole, disorders caused by their deficiency. Fat-soluble(liposoluble) vitamins as drugs and antioxidants.

Membrane structure (Sanger-Nicolson) and functions. Com-position and characteristics of membrane components, their pro-perties and diversity, selective permeability and transport substan-ces through the cell membranes.

Digestive mechanism for the lipids and absorption in gastro-intestinal tract. Structure, functions and metabolism of the bileacids. Re-esterification, formation of chylomicrons, transport. Li-poproteins metabolism, clinical disorders of lipoproteins metabolism.

Lypolysis of triacylglycerols in tissue: enzymic steps, hormo-nal control of lipolysis in the different tissues and its disorders.

Fatty acid b-oxidation: reactions, enzymes and coenzymes,final products, high-energy phosphate (ATP) production, stoichio-metry of b-oxidation. The specific behaviour of odd-numbered andunsaturated fatty acids. Alternative pathways for the fatty acid oxi-dation.

Glycerol oxidation: the enzymic steps, ATP production, inter-relation with glycolysis.

Biosynthesis of fatty acids: characteristics of polyenzymaticcomplex, steps, source of acetyl-CoA and NADPH+.

Ketone bodies metabolism: nature of the ketone bodies, keto-ne bodies production and oxidation. Energy (ATP) production du-ring oxidation of the ketone bodies. Ketoacidosis.

Cholesterol metabolism: site, steps and carbon sources for itssynthesis. The first step of the cholesterol synthesis (to mevalonicacid), regulation. Esterification of cholesterol as precursor of othercompounds (bile acids, steroid hormones and vitamins). Choles-terol excretion from the human organism. Connection betweencholesterol and blood plasma lipoproteins metabolism. Disordersof the cholesterol metabolism: hypercholesterolemia, cholelithiases(gallstones formation) and atherosclerosis.

Phosphoglycerides metabolism. Biosynthesis de novo and sal-vage pathway: reactions, regulation, lipotropic factors. Convertion

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of phosphatidylserine to other phospholipids (phosphatidylethano-lamine, phosphatidylcholine). Modification and oxidation of phos-pholipids.

Sphingolipid’s, chemical structure, biorole. Sphingolipids’biosynthesis: formation of sphinganine, ceramide, sphingomyelin,glycosphingolipids. Catabolism of sphingolipids. Lipidoses due toimpaired ganglioside catabolism. Disorders of sphingomielin me-tabolism (Niemann-Pick, Gaucherie, Fabry diseases).

Prostaglandins and related compounds: general features andbiologic role, nomenclature, structure and biosynthesis. Biologicalrole in health and pathology.

Disorders linked to lipid metabolism: dislipemia and lipidoses.

Chapter VII

METABOLISM OF SIMPLE AND CONJUGATED PROTEINS

Protein turnover. The amino acid pool: notion inputs and out-puts. Essential amino acids. Nitrogen balance, its types.

Proteins digestion: role of HCl and proteolytic enzymes(endo- and exopeptidases). Proteases: secretion, mechanism activa-tion, regulation and specificity. HCl role, mechanism of secretionand its regulation. Gastric juce acidity assay: hypochlorhydria,hyperchlorhydria. Amino acids absorption into small intestine:Na+-simport mechanism and g-glutamate cycle. Bacterial putrefa-ction of the amino acids in large intestine: production of toxiccompounds (indol, scatol, cresol, cadaverine, putrescine, etc.) andtheir inactivation in the liver. Mechanism of conjugation, produc-tion of indicane, its diagnostic means. Examination of the antitoxicfunction of the liver.

Proteolysis (catabolism) of proteins in the tissues, its regulation.Amino acids degradation (intracellular catabolism). The dis-

posal of amino acids nitrogen: oxidative deamination (direct andindirect), enzymes, coenzymes, biologic role.

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Transamination of the amino acids; role, enzymes, coenzymesand mechanism of the reaction. Medical usage of aminotransfera-ses' activity assay: alanine transaminase (ALT) or glutamic pyru-vic transaminase (GPT) and aspartate transaminase (AST) or gluta-mic oxaloacetic transaminase (GOT).

Amino acids decarboxylation, enzymes, coenzymes, final pro-ducts. Biogenic amines: serotonine, histamine, dopamine andg-aminobutyric acid (GABA), their biological activity and inacti-vation. The fate of the amino acids carbon skeletons.

Ammonia production and toxicity. Overall flow of nitrogen.The urea cycle, reactions, regulation and importance. Interrelation-ship between urea and TCA (Krebs) cycles.

Specific metabolic pathways of amino acids: gly, ser, thr, cys,met, phe, tyr, trp, glu, asp. Amino acids as major inputs to the one–carbon pool and precursors of biological important compounds.

Molecular diseases associated with abnormal amino acidmetabolism (molecular diseases): Hartnup’s disease, phenylketo-nuria, tyrosinemia, alkaptonuria, maple syrup urine disease, etc.

Nucleoprotein metabolism: digestion and absorption in smallintestine. Nucleotide turnover. De novo synthesis of purine andpyrimidine nucleotides: substrates, pathways, regulation. Deoxyri-bonucleotide formation. Salvage pathway for purine and pyrimi-dine bases. Conversion of the MNP to DNP and TNP. Degradationof purine and pyrimidine nucleotides. Diseases associated withdefects of nucleotide metabolism (gout, orotic aciduria).

Hemoprotein metabolism. Digestion and absorption of hemo-globin in gastro-intestinal tract. Biosynthetic pathway of the hemeand hemoglobin, regulation of the hemoglobin synthesis. Drugs asactivators of the hemoglobin synthesis. Hemoglobin degradation inthe tissues. Iron (Fe) metabolism. Genetic disorders of the hemebiosynthesis (porphyrias). Hiperbilirubinemia and jaundices, types,biochemical diagnostics.

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Chapter VIII

HORMONES

The hierarchy of the regulatory systems in the human orga-nism. Hormone’s place in the hierarchy of the metabolism re-gulation and physiological functions.

Classification and mechanisms of hormone’s action. Thehormone-receptor interaction. The receptor-adenylate cyclase com-plex: 3’,5’-cyclic AMP function, cyclic AMP-dependent proteinkinase and phosphorylation of the cellular proteins. Diacylglyceroland inositol-1,4,5-triphosphate – the second messengers of the hor-mones. Role of protein kinase and Ca2+ in hormonal function.Calmodulin – structure and role. General mechanisms of hormonesbiosynthesis, release and their regulation. Central regulation of thehormone functions: role of hypothalamus (neurohypophysis) andadenohypophysis.

Hypothalamic hormones: liberins (releasing hormones, RH)and statins (releasing inhibiting hormones, RIH), chemical structu-re, biological role.

Hypophyseal (pituitary) hormones: representatives (somato-tropin, corticotropin, thyrotropin, et al.), structure, function, di-sea-ses associated with pituitary disorders and their correction.

Vasopressin and oxytocin: chemical structure, metabolic effe-ctts. Diabetes insipidus, its manifestations. Utility of oxytocin inmedicine.

Thyroid hormones: T3 and T4, structure, biosynthesis, mecha-nism of action, release, transport, metabolic effects, disorders.

Parathyroid hormones: structure, biosynthesis, mechanism ofaction, release, transport, metabolic effects. Interrelation of para-thyrin with other compounds, that regulate calcium and phosphatemetabolism. Role of 1,25-dihydroxycholecalciferol for parathyroidhormone action. Disorders of parathyroid glands functions.

Pancreatic hormones: insulin and glucagon, structure, biosyn-thesis, mechanisms of action, release, transport, metabolic effects.

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Mechanism activation and inactivation of insulin. Diabetes melli-tus: causes, types (I and II), metabolic changes in the patients andtheir correction.

Catecholamine hormones (adrenalin, noradrenalin): structure,biosynthesis, release, transport, metabolic effects, disorders.

Glucocorticoids hormones: structure, biosynthesis, release,transport, metabolic effects, disorders. Steroid diabetes, metabolicdisorders.

Mineralocorticoids hormones: structure, biosynthesis, release,transport, metabolic effects, disorders.

Sexual hormones (androgens, estrogens): structure, biosynthe-sis, release, transport, metabolic effects, disorders.

Utilisation of hormones and antihormones as drugs in medici-ne for substitution therapy and pathogenetic therapy.

Chapter IX

BLOOD

Blood functions and physico-chemical properties.Blood cells: peculiarities of the composition, metabolism of

erythrocytes, leucocytes, lymphocytes and thrombocytes. Function– metabolism relationships.

Plasma organic compounds: proteins and enzymes, non-pro-teic nitrogen substances, residual nitrogen, carbohydrates, lipidsand organic acids. The major proteins of blood plasma: brief cha-racteristics, methods of separation and assay. Hypo-, hyper-, dis-and para-proteinemias: notion, causes and examples. Oncotic pres-sure and its disorders, reasons and correction.

Blood enzymes: classifacation, practical utility. Indicator (or-gan specific) blood enzymes in liver and heart diseases. Mecha-nism of enzymes’ level increasing in the blood serum.

Plasma non-proteic nitrogen compounds. Hyperammonemiaand hyperuremia, causes, consequences. Bilirubin: types, forma-

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tion, excretion in the healthy human organism. Disorders of hemo-globin’s catabolism: icteric syndrome (types, causes, disorders ofbilirubin conjugation, its excretion and clinical laboratory diagnos-tics).

Inorganic compounds: the major anions, cations and microele-ments, their role.

Mechanisms of oxygen and CO2 transport, biochemical me-chanisms of respiration function of blood. Functional requirementsto hemoglobin and cooperative binding of oxygen, role of 2,3-diphosphoglycerate in this process. Role of carboanhydrase in ga-ses transport in the blood. Disorders of gas transport (mechanisms,diseases). Hypobaric and hyperbaric oxygenation, its usage in me-dicine.

Acid-base equilibrium: buffer systems and physiological me-chanisms of buffering. Disorders of acid-base equilibrium of theblood: alkaloses and acidoses, types, diagnostics and mechanismsof buffering correction.

Fluid-coagulation equilibrium. Biochemical mechanisms ofblood clotting: plasmic and platelets coagulation factors (brief cha-racteristic). Extrinsic and intrinsic mechanisms of blood clotting:causes, timing and cascade mechanism. Fibrinolitic and anticoagu-lant mechanisms. Natural and synthetic anticoagulants, their me-chanism of action and usage in medicine. Role of vitamins K andD in the blood coagulation. Native and synthetic anticoagulants(antivitamins K: pelentan, dicumarol, etc.), utility in medicine.

Chemical components of the blood as drugs (albumin, gam-ma-globulin, interferon, etc.).

Chapter X

STOMATOLOGICAL BIOCHEMISTRY: CONNECTIVE, BONEAND DENTAL TISSUES. BIOCHEMISTRY OF SALIVA

Types and functions of the connective tissue. Main componen-ts of the connective tissue: cells (representatives, biological role)

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and extracellular matrix (structural elements and their biologicalrole).

Fibrilar proteins of the connective tissue (collagen, elastin):the particularities of chemical composition, structure and proper-ties. The peculiarities of collagen biosynthesis, post-synthetic(post-translation) modifications and degradation.

Glucosamine glycans (heteropolysaccharides or mucopolysa-ccharides) of the extracellular matrix of the connective tissue:main representatives, their structure, biological role. Proteoglycansand glycoproteins, their biological role.

Physiological and pathological modifications of the connecti-ve tissue metabolism: age-dependent modifications, acquireddisorders (hypovitaminosis C, diabetes mellitus). Genetic disor-ders: collagenoses, mucopolysaccharidoses, biochemical manifes-tations.

Structure and role of the bone tissue. The cells of the bonetissue: the representatives, their biological role. Organic com-pounds of the bone tissue: fibrilar and non-fibrilar proteins, proteo-glycans, carbohydrates, lipids.

Mineral components of the bone tissue: main anions, cations,their structural organization, minor ions, olygoelements. Appatite:components, structure and properties.

Bone formation and resorbtion: cells, that participate in theseprocesses, the stages and mechanisms of the processes. Regulationof the bone tissue metabolism in the human organism. Role of thethyroid and parathyroid glands’ hormones and vitamins D and Cfor the bone metabolism. Pathology of the bone metabolism: age-dependent, osteoporosis.

Dental tissues: general characterization and role. Teeth tissues(enamel, dentine, cementum) structural organization and generalcharacteristics. Organic and mineral components of dental tissues.Normal biochemical processes in the teeth. Role of vitamins A, D,C in the metabolism of dental tissues and the soft tissues of themouth. Calcium, phosphorus and fluor metabolism: main alimen-

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tary sources, mechanisms of absorption into intestine, blood trans-port, excretion, role in the dental tissue metabolism and in the teethpathology.

Biochemical processes that take place during the dental cariesdevelopment.

Periodontium: the main chemical compounds, their characte-ristics and biological role. Physiological biochemical processes ofthe periodontal tissues. Biochemical processes that take place inthe pathology of the periodontium, role of the inflammation media-tors and immune system. Dental plaque: chemical composition,main biochemical processes in the plaque, the correlation with theperiodontal pathologies (gingivitis, parodontitis, parodontosis).

Gingival liquid: causes of the apparition, chemical composi-tion and its role.

Saliva: sources, chemical composition, physico-chemical pro-perties and role. Clinical diagnostic means of the salivary compo-nents for medicine and dentistry.

Chapter XI

PHARMACEUTICAL BIOCHEMISTRY METABOLISMOF DRUGS. PHOTOSYNTHESIS

Natural biological active peptides: anserine, carnosine, angio-tensine, secretin, endothelin, hormones. Antibiotics as protein deri-vatives.

Biological role of water in the human organism (functionaland structural one). Physico-chemical properties of water. Water assolute for natural substances and xenobiotics.

Metabolism of drugs and xenobiotics in organism. Relationbetween metabolism of the drugs and their chemical structure.Localization of the drug metabolism in the organism (enteral,extracellular, cellular). Stages of the xenobiotics metabolism (mo-dification and cojugation).

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Conjugation of xenobiotics: I type (glucuronide, sulphate,acetyl conjugations) and II type (a prior activation of the substrate-xenobiotic) conjugation. Enzymes involved in the metabolism ofxenobiotics in the human organism. Metabolism of drugs andtoxins (poisons).

Microsomal oxidation of substances and xenobiotics (mono-oxigenase and reductase chains). Role of cytochrome P450 in thisprocess. Drugs-activators of cytP450 production in the organism.Conditions for drug metabolism. Biotechnology of drugs. Bioche-mical methods used in drug standardization and quality control.

Photosynthesis and characteristics of the photosynthetic stru-ctures – chloroplasts. Chlorophyll (major structural characteristics)and its role in photosynthesis.

Photosynthesis basis: mechanism of the light (photochemical)and dark (synthetic) stages. Cyclic and noncyclic transport of ele-ctrons in the photochemical stage of the photosynthesis. Waterphotolysis, Hill reaction. The role of photosystems I and II in thephotosynthesis.

Photophosphorylation (ATP production in chloroplasts) andoxidative phosphorylation in mitochondria, common characteris-tics and differences. The role of the Calvin cycle in the synthesisof polysaccharides. Photosynthesis as a way for the buildup of theproducts with therapeutic properties (alkaloids, flavonoids, poly-phenols, steroids, etc.).

AMINO ACIDS. CHEMICAL STRUCTURE OF PROTEINS.ENZYMES

1.5. 0,0,1,0,0Which compounds are structural units of simple proteins andwhat type of linkage does connect these structural elements?A. Mononucleotides b-glycosidicB. Glucose ester

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C. Amino acids peptideD. Fatty acids etherE. Glycerol disulfide

2.5. 0,1,1,0,1Which of the groups of amino acids are present in the proteinsand what are their characteristics?A. Hydroxyamino acids refer to the D-seriesB. Thioaminoacids refer to the L-seriesC. Heterocyclic amino acids are a-amino acidsD. Diamine dicarboxylic amino acids are b-amino acidsE. Diamine monocarboxylic amino acids have optical activity

3.5. 1,0,1,0,0Tryptophan:A. is a heterocyclic amino acidB. is a homocyclic amino acidC. contains the heterocycle of indoleD. contains the heterocycle of imidazoleE. has acidic properties

4.5. 1,0,0,1,1For methionine and threonine the following statements arecorrect:A. their pI is in the neutral zone of рНB. they have one asymmetric cаrbon-atomC. they have identical functional groups in the structureD. they are derivatives of the butyric acidE. they are essential amino acids

5.5. 0,1,0,0,0The amino acids of arginine and lysine have the followingcommon properties:A. contain the guanidine residue

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B. have a positive charge at the physiological рНC. are derivatives of the capronic acidD. have several asymmetric carbon atomsE. form peptide bonds using both amino groups

6.5. 1,1,0,1,0The total charge of proteins depends on:A. amino acids structureB. pH of the solutionC. b-COOH and g-NH2 groups of the polypeptide chainD. COOH and NH2 groups of the amino acids radicalsE. hydrophobic radicals

7.5. 0,0,1,1,1Which of the statements about protein denaturation are co-rrect?A. Destruction of primary structure increase of the biological

activityB. No changing in the protein activity increase of the hydrophilityC. Destruction of tertiary structure increase of the hydropho-

bityD. Destruction of quaternary structure decrease of the biological

activityE. No changes in the primary structure changes in the form of mo-

lecules

8.5. 0,1,1,1,1Сolloidal solutions of the proteins have the following proper-ties:A. increased speed of diffusionB. low osmotic pressureC. insignificant diffusion rateD. high viscosityE. optical properties

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9.5. 1,1,0,0,1The primary structure of proteins:A. represents a sequence of amino acidsB. is determined geneticallyC. is stabilized by weak and noncovalent bondsD. is broken after denaturationE. is broken after hydrolysis

10.5. 1,1,1,0,0The correct statements concerning the peptide bond:A. each peptide bond forms 2 hydrogen bondsB. it exists in two resonant formsC. atoms O and H are situated in trans-position with regard to the

bond C-ND. the bonds of a-carbon atom forbid the free rotationE. the atoms of the peptide bond and 2 a-carbon atoms are situated

in the same plane

11.5. 0,0,1,1,0Secondary structure of proteins:A. is stabilized by hydrophobic and ionic interactionsB. there is only a-spiral or only b-structureC. is a result of the interaction of closely located radicals of amino

acidsD. is stabilized by hydrogen bondsE. the bonds are formed within the limits of one chain only

12.5. 0,1,0, 1,1Secondary structure of proteins:A. appears at the interaction of the closely situated chains onlyB. represents a-spiral and b-structureC. is stabilized by disulfide bonds between the methionine radicalsD. is stabilized by disulfide bonds between the cysteine radicalsE. appears at the interaction within a single chain or between two

closely situated chains

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13.5. 1,0,1,0,1Tertiary structure of proteins:A. is packing of the polypeptide chain is in three-dimensional

spaceB. is stabilized by covalent bondsC. is determined by the sequence of amino acids, their form and

polarityD. does not cause biological activityE. is broken at denaturation

14.5. 1,1,0,0,0Quarternаry structure of proteins:A. is the result of protomers interaction with the formation of the

functional proteinB. is the result of the interaction of the contact surfaces of domainsC. is stabilized by covalent bondsD. does not collapse at denaturationE. the protein molecule has mobility

15.5. 0,1,1,1,0The following proteins have the quarternаry structure:A. mioglobinB. hemoglobinC. fibrinogenD. lactate dehydrogenase (LDH1)E. serum albumin

16.5. 1,0,0,1,0The correct statements about enzymes:A. are biological catalystsB. are inorganic catalystsC. exist only in an active formD. in organism exist also in an inactive formE. catalyze only reactions of synthesis

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17.5. 1,1,0,0,1General properties of both enzymes and non-biological catalystsare:A. don’t change the direction of reactionB. don’t change the equilibrium of a reversible reactionC. catalyze the reaction in mild conditionsD. catalyze the reaction in both directionsE. not spent during reaction

18.6. 0,1,1,1,0Enzymes differ from inorganic catalysts by that they:A. accelerate thermodynamically possible reactionsB. have specificityC. have a much greater catalytic efficiencyD. catalyze the reactions in mild conditionsE. reduce the energy of activation for the chemical process

19.5. 1,0,1,1,1The active center of an enzyme represents:A. a unique complex of three-dimensional structureB. a point in the tertiary structureC. a cofactor enters in the structure of the active centerD. the active center consists of catalytic and contact sitesE. the substrate is connected in the active center

20.5. 0,1,1,1,0The correct statements about the mechanism of enzymes’ action:A. Substrate isn’t changed in the enzyme-substrate complexB. Substrate is deformed in the enzyme-substrate complexC. The complementarity of the active centеr is induced by the sub-

strateD. Enzyme-substrate complex reduces the substrate’s entropy,

promoting the achievement of a transitive stateE. Enzyme-substrate complex raises the entropy

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21.5. 1,1,0,0,1The primary structure of proteins is:A. represented as a sequence of amino acidsB. determined geneticallyC. stabilized by weak and noncovalent bondsD. broken at denaturationE. broken at hydrolysis

22.5. 1,1,1,0,0The correct statements concerning the peptide bond:A. Each peptide bond forms 2 hydrogen bondsB. It exists in two resonant formsC. Atoms O and H are situated in trans-position with regard to the

bond C-ND. The bonds of a-carbon atom forbid the free rotationE. The atoms of the peptide bond and 2 a-carbon atoms are situa-

ted in the same plane

23.5. 0,0,1,1,0Secondary structure of proteins:A. Is stabilized by hydrophobic and ionic interactionsB. There is only a-spiral or only beta-structureC. Is a result of the interaction of closely located radicals of amino

acidsD. Is stabilized by hydrogen bondsE. The bonds are formed within the limits of one chain

24.5. 1,0,1,0,1The correct statements about the chemical nature of enzymes:A. The main its components are amino acidsB. Enzymes are thermostable compoundsC. They form colloidal solutions in waterD. Enzymes are micromolecular compoundsE. They can be degraded by proteases

26

25.5. 1,1,0,1,0The correct statements about the mechanism of enzyme action:A. It reduces the energy of activation of the reactionB. An enzyme-substrate complex is formedC. Enzyme-substrate complex is a stable, rigid structureD. Enzyme-substrate complex is an unstable structureE. The formation of enzyme-substrate complex does not change

the physical properties of the enzyme

26.5. 0,1,1,1,0The correct statements about the mechanism of enzyme action:A. Substrate isn’t changed in the enzyme-substrate complexB. Substrate is deformed in the enzyme-substrate complexC. The complementarity of the active centеr is induced by the sub-

strateD. Enzyme-substrate complex reduces the substrates entropy,

promoting the achievement of a transitive stateE. Enzyme-substrate complex raises entropy, increasing the level

of the substrate freedom

27.5. 0,0,1,1,1Specificity of enzymes:A. depends on coenzymeB. depends both on protein and coenzymeC. can be absolute: the enzyme catalyzes the transformation of

only one substrateD. can be relative: the enzyme catalyzes the transformation of

several substrates with an identitic chemical bondE. depends on apoenzyme

28.5. 1,0,0,0,1Allosteric centеr is:A. separated spatially from the active centеrB. a place of substrate binding

27

C. characteristic for all enzymesD. the place for binding the compounds that have structural simila-

rity to the substrateE. a place of metabolites, ligands binding

29.5. 1,0,1,0,0Allosteric enzymes, the correct statements:A. consist of two or more protomersB. can have only one active and one allosteric centеrC. the allosteric centеr can join both the activator and the inhibitorD. the modulators are joined by covalent bonds to allosteric centеrsE. reaction kinetics is identical for allosteric and usual enzyme

30.5. 0,0,1,0,0The free COOH-group and NH2-group are present in:A. simple lipids complex proteinsB. carbohydrates lipidsC. amino acids nitrogenous basesD. nitrogenous bases nucleotidesE. nucleotides homopolysaccharides

31.5. 1,0,1,1,1Which of the following substances are biopolymers?A. simple proteins nucleosidesB. neutral lipids amino acidsC. glycogen DNAD. DNA mRNAE. mRNA proteins

32.5. 1,0,1,1,0Which of the following statements about serine are correct?A. has one asimmetric C-atomB. has isoelectric point in acidic mediumC. has isoelectric point in neutral mediumD. is an nonessential amino acidE. is an essential amino acid

28

33.5. 0,1,0,1,1The correct statements for arginine:A. has negative electric charge on pH=3B. has electric point in basic mediumC. hydroxyarginine present in collagen structureD. is a polar amino acidE. guanidine presents in arginine’s composition

34.5. 0,0,1,1,0The correct statements for lysine:A. has 2 asimmetric C-atoms in its structureB. is a nonessential amino asidC. moves to catod in solution with physiological pHD. may be hydroxylized during posttranslation modificationsE. has two negative electric charges on pH=8

35.5. 1,1,1,0,1The correct statements for glutamic acid:A. doesn’t have electric charge on pH=8B. amid is product of glutamic amino acid aminationC. moves to catod into solution with physiological pHD. is a diaminoderivative of succinic acidE. is an aliphatic amino acid

36.5. 0,0,0,1,0Which of amino acids solution (pH=2.0) has a positive electriccharge?A. Glu, Asp, SerB. Glu, Pro, TyrC. Pro, Val, ClnD. Lys, Arg, GlyE. Cys, Met, Tyr

29

37.5. 0,0,1,0,0Isoelectric point of tetrapeptide Glu-Asp-Cys-Ser is on pH:A. 1,0-2,5B. 2,6-3,5C. 4,0-4,5D. 6,8-7,4E. 7,6-8,2

38.5. 0,0,1,0,0Which of amino acids solution (pH=8.0) has a great negativeelectric charge?A. Glu, Pro, TyrB. Pro, Val, GlyC. Lgu, Ala, AspD. Lys, Arg, HisE. Cys, Met, Trp

39.5. 1,0,0,0,0Which of the statements are correct for histidine and tryptophan?A. They are heterocyclic amino acidsB. They have positive electric charge on physiological pHC. They have 2 N-atoms in moleculesD. They have 2 asymmetric centersE. They are present as hydroxyamino acids in the proteins

40.5. 0,1,1,0,0For identification of N-ending amino acid is used:A. hidrazinB. F-dinitrobenzenC. phenylisotiocianateD. trypsin, pepsinE. chymotrypsin

30

41.5. 0,1,0,0,0For identification of C-ending amino acid is used:A. ureaB. carboxylases A and BC. guanine’s hydrochlorideD. perphormin acidE. p-dimethyl-aminobenzaldehyde

42.5. 0,1,1,1,1The correct statements for proteins:A. they are the main energetic substratesB. they are components of cell membranesC. they are biocatalystsD. they are regulators for oncotic pressure of bloodE. they have transport function

43.5. 1,1,0,1,1The correct statements according to the primary structure ofprotein:A. sequence of amino acidsB. determined by genomeC. stabilized by noncovalent bondsD. hydrolysis breaks itE. the high levels of proteins organization is based on its structure

44.5. 1,0,0,0,0The correct statements for secondary structure of protein:A. has a definitive conformationB. stabilizes by hydrophobic and iones interactionsC. presents only a-helixD. presents only b-structureE. chemical bonds form only into one chain

31

45.5. 1,0,1,0,1According to a-helix, the following statements are correct:A. predominates in globular proteinsB. predominates in fibrilar proteinsC. is a symmetric helixD. hydrogen bonds form between CO-group and NH-group of

different polypeptide chainsE. hydrogen bonds form between CO-group and NH-group of

one polypeptide chain

46.5. 0,0,1,0,0Tertiary structure of protein, the correct statements:A. is stabilized by covalent bondsB. is a result of spatial connections of nearest amino acidsC. is a result of accidental connections of amino acids and H2O

radicalsD. is an absolute strong structureE. includes only a-helix

47.5. 1,0,0,0,0According to quarternary structure of the protein, the follo-wing statements are correct:A. a2b2 are protomers of HbA2B. H2M2 are protomers of LDH1 isoenzymeC. H3M1 are protomers of LDH5 isoenzymeD. a2g2 are protomers of HbA1E. S-S-bonds there are between protomers

48.5. 0,1,1,1,0The correct statements about the chemical structure of humanhemoglobin (Hb):A. is tetramer of 4 a-subunitsB. is tetramer of two types subunitsC. a prosthetic hemo-group is on each of its subunit

32

D. connection between heme and protein is based on the Fe2+-his-bond

E. is a dimer of two b-subunits

49.5. 1,0,0,0,0Collagen, the correct statements:A. includes about 1/3 of glycineB. almost doesn’t include alanineC. polypeptide chain composes a small content of amino acidsD. polypeptide chain has a-helix conformationE. is disolved in water

50.5. 0,0,1,0,0Enzymes are:A. only simple proteinsB. glycolipidsC. macromoleculesD. only nucleoproteinsE. heteropolysaccharides

51.5. 1,1,0,0,0Cofactors are:A. cations of certain metalsB. derivatives of vitaminsC. anions of certain metalsD. lipidsE. only easily dissociated components

52.5. 0,0,0,0,1Mechanism action of enzyme (E):A. a strong complex forms between substrate (S) and active center

of enzymeB. structure of S can not change on active center of EC. during connection S with E only conformation of S changes

33

D. during connection S with E only conformation of E changesE. during connection S with E both conformations of E and S

change

53.5. 0,0,0,1,0Specificity of carboanhydrase:A. is relativeB. is a relative groupC. is stereochemicalD. is absoluteE. it doesn’t have specificity to chemical bond

54.5. 0,1,0,0,0Alcohol dehydrogenase specificity:A. is relativeB. is a relative groupC. is stereochemicalD. is absoluteE. it doesn’t have the substrate specificity

55.5. 1,0,1,0,1The correct statements about pepsin and its activity regula-tion:A. is hydrolaseB. is lyaseC. is prodused during partial proteolysis of pepsinogenD. partial proteolysis is a reversible processE. partial proteolysis is an irreversible process

56.5. 1,0,0,0,1The correct statements about a-amylase:A. is hydrolaseB. is lyase

34

C. during activation process the primary structure of enzymechanges

D. NaCl is a denaturative agent for a-amylaseE. NaCl is an activator for a-amylase

57.5. 1,0,0,0,0Sulfanylamides action mechanism for enzymes:A. They are competitive inhibitorsB. They are reversible competitive inhibitors for bacteria enzymesC. They change the primary structure of the enzymeD. They are noncompetitive inhibitorsE. They act as allosteric inhibitors

58.5. 0,0,1,1,1Which type of chemical reaction is specific for LDH?A. isomerizationB. hydrolysisC. convertion of pyruvic acid to lactic acidD. convertion of lactate to pyruvateE. oxido-reduction

59.5. 1,0,0,0,0Which of the following statements are correct for LDH-isoen-zymes?A. They are tetramers of two types “M” and “H”B. They are dimers of two types “M” and “H”C. Their chemical reaction is irreversibleD. Isoenzymes of blood plasma are produced in the liverE. Isoenzymes of blood plasma are produced in the heart

60.5. 1,0,1,1,0The correct statements about vitamin B2 (riboflavin):A. FMN is a complex monophosphate ether of vitamin B2B. FAD is dinucleoside of vitamin B2

35

C. vitamin B2 includes isoalloxazinic heterocycleD. FMN and FAD are coenzymes of oxido-reductasesE. only FMN is a coenzyme of oxido-reductases

61.5. 1,0,1,1,0For NADP+ is correct:A. NADP- dependent enzymes participate in anabolic processesB. this is a reduce form of coenzymeC. this is an oxidized form of coenzymeD. active portion of coenzyme is amid of nicotinic acidE. it includes Cu2+-ion

62.5. 0,0,1,0,0Vitamin B6 and its coenzymes:A. coenzyme is only pyridoxamineB. it is coenzyme for some oxido-reductasesC. both its forms, pyridoxal phosphate and pyridoxamine phos-

phate, participate during transaminationD. in pyridoxal phosphate its aldehyde group is phosphorilatedE. it is coenzyme only for transamination

63.5. 1,0,0,0,1Vitamin B12 is a coenzyme for the following reactions:A. methylmalonyl-SkoAà succinyl-SkoAB. pyruvateà oxaloacetateC. prolineà hydroxyprolineD. succinateà fumarateE. homocysteineà methionine

64.5. 1,0,0,0,0Ascorbic acid is:A. used in hydroxylation reactions in the presence of O2B. a precursor of HS-coA

36

C. a coenzyme for conversion of noradrenalin to adrenalinD. deposited only in the liverE. used during convertion of Ser to Gly

65.5. 0,0,1,1,1Zn-containing enzymes are:A. cytochrome oxidaseB. glutathione peroxidaseC. alcohol dehydrogenaseD. carboanhydraseE. RNA- and DNA-polymerases

66.5. 1,1,1,0,1Biologically active peptides (for animals) are:A. liberins and statinsB. angiotensinsC. secretin and gastrinD. aldosteroneE. endotheline

67.5. 1,1,1,0,0Antibiotics – peptides:A. cycloserineB. azaserineC. penicillinD. thyreoliberinE. somatothropin

NUCLEIC ACIDS. PROTEIN SYNTHESIS

1.5. 0,1,0,1,1The main nitrogenous bases of DNA are:A. 5-methylcytosineB. cytosine

37

C. 2-methyladenineD. guanineE. thymine

2.5. 1,0,1,0,1The main nitrogenous bases of RNA are:A. adenineB. xantineC. guanineD. thymineE. uracil

3.5. 0,1,1,1,0The structural components of DNA are:A. dihydroxyuracilB. deoxyriboseC. phosphoric acidD. thymineE. ribosylthymine

4.5. 0,1,0,0,1The structural components of tRNA are:A. inosineB. pseudouridineC. thymineD. deoxyriboseE. adenine

5.5. 0,1,1,0,0The following chemical bonds are in the nucleic acids:A. peptide bondB. 3’,5’- phosphodiesterC. N-glycosidic

38

D. disulphidicE. ester

6.5. 1,0,1,0,1According to the secondary structure of DNA, it is correct:A. it is the double helixB. the chains are combined by the phosphodiester bondsC. the nitrogenous bases protrude into the interior of the helixD. the chains don’t separate at a high temperatureE. it doesn’t have anticodon sites

7.5. 0,1,0,1,1For RNA, it is correct:A. the cellular RNA content is constantB. is a single-stranded ribonucleotideC. is composed of AMP, GMP, TMP, CMPD. the RNA-chain is polarE. the nucleotides are combined by 3’,5’-phospho-diester bonds

8.5. 1,0,0,1,0For mRNA, it is correct:A. it transfers the genetic information from nucleus to ribosomesB. is the double-chain polynucleotideC. the 5’-end contains the CCA sequenceD. it contains the methyl-containing basesE. it has a small molecular mass

9.5. 1,1,0,0,1The typical characteristics of DNA biosynthesis:A. replication is semiconservative processB. it needs the presence of mDNA double-chainC. a primer is not necessaryD. deoxyribonucleoside phosphates are only necessaryE. nucleus is the place for DNA synthesis

39

10.5. 0,1,1,1,0Transcription:A. the entire chromosome works simultaneouslyB. is asymmetricC. only certain DNA sites workD. the double-helix of DNA is templateE. template is the noncodogenic DNA chain (-)

11.5. 0,0,1,1,0The common characteristics of DNA and RNA biosynthesis:A. using the deoxyribonucleoside triphosphatesB. using the ribonucleoside triphosphatesC. the motive power of elongation is pyrophosphate hydrolysisD. the synthesis of chains goes in 5’ to 3’ directionE. the conservation of DNA template

12.5. 0,1,0,0,1The RNA processing is:A. Okazaki fragments bindingB. the 7’-methylguanine connection with 5’-endC. the addition of CCA-sequenceD. the place for processing is cytosolE. nucleus is site for RNA processing

13.5. 1,0,0,0,1Genetic code:A. is the tripletB. is the singletC. codons are read in 3’ to 5’ directionD. on mRNA the codons are divided by nonsense codonsE. cod is degenerate (redundant)

40

14.5. 0,1,0,1,1According to translation, it is correct:A. synthesis of polypeptide chain starts on the C-endB. synthesis of polypeptide chain starts on the N-endC. initiative amino acid for procaryotes is methionineD. donor of formyl is the N10-formyl-FH4 (tetrahydrofolic acid)E. formation of formyl-tRNA is catalized by specific transformy-

lase

15.5. 1,0,1,0,1For the elongation of protein biosynthesis, it is correct:A. formation of peptide bondsB. connection of met-tRNA on the P siteC. using the 2 GTP moleculesD. formation of a peptide bond between NH2-group of the P

center and COOH-group of the A centerE. ribosome’s moving on one codon of mRNA

16.5. 0,1,0,0,1Regulation of the anabolic vital cell processes is dependent on the:A. presence of inductive enzymesB. presence of repressive enzymesC. presence of the constitutive enzymesD. coordinative inductionE. coordinative repression

17.5. 0,1,1,0,1Enzymic characteristics for telomerases:A. enzyme has a small activity “in vitro”B. the human enzyme has a high activityC. process is dependent on the length primerD. the primers are smaller than 10 nucleotidesE. when the primer is more than 10 nucleotides, the DNA can have

thousands of nucleotides

41

18.5. 1,0,1,1,0Induction and repression of enzymes:A. induction is determined by the “de novo” synthesis of the enzy-

mic moleculesB. repression is an analog of retroinhibitionC. repression and induction are based on the economic principle

in the cellD. repression is the inhibition of enzyme synthesisE. induction doesn’t define the new synthesis of enzyme molecu-

les

19.5. 1,1,1,1,1Mechanisms of organism ageing:A. production of anomalous chromosome is increasedB. chromosomes loss predominatesC. gene extraction near telomerase takes placeD. after extraction of this gene the ageing repressor is inactivatedE. the telomer binding proteins (TBP) are included in process

20.5. 1,0,0,1,0The confirmations about thymidine are correct:A. it is a deoxyribonucleosideB. it has only the lactim formC. it contains two N1-glycoside bondsD. it has the N1-C1-glycoside bondE. it has the molecular structure C9H11O5N2

21.5. 1,0,0,1,1For the adenilic acid, it is correct:A. it consists of nitrogenous base, pentose and phosphateB. it is a deoxyribonucleotideC. it has an a-glycoside bondD. it is AMPE. it is cAMP

42

22.5. 1,1,0,1,0For mRNA, it is correct:A. has the structure of the “clover leaf”B. an amino acid is composed with 3’-OH of adenine nucleotideC. an anticodon loop consists of 3 nucleotidesD. an anticodon loop consists of 7 nucleotidesE. it contains about 50-60% of all RNA content of the cell

23.5. 1,1,0,0,0The Okazaki fragments:A. these are the short DNA fragmentsB. are sintetized in the 5’ to 3’ directionC. these are noninformative DNA sitesD. are sintetized in the 3’ to 5’directionE. are formed on the leader DNA chain during replication

24.5. 0,1,0,1,1Codon AUG is the:A. codon for cysteineB. initiative codon for translationC. initiative codon for transcriptionD. codon for methionineE. codon for formyl-methionine

25.5. 1,0,0,1,1Choose the inhibitor for the replication:A. streptomycinB. erythromycinC. puromycinD. mitomycin CE. canamycin

26.5. 0,1,0,1,1The main nitrogenous bases of DNA are:A. 5-methylcytosine

43

B. cytosineC. 2-methyladenineD. guanineE. thymine

27.5. 1,0,0,0,1The main nitrogenous bases of RNA are:A. adenineB. 1-methylguanineC. hypoxantineD. thymineE. uracil

28.5. 1,0,1,0,0The minor nitrogenous bases of nucleic acids are:A. thioguanineB. 2,6,8-trioxypurineC. N2-dimethylguanineD. 2,4-dihydroxypyrimidineE. 4-amino-2-hydroxypyrimidine

29.5. 0,1,1,1,0The structural components of DNA are:A. dihydroxyuracilB. deoxyriboseC. phosphoric acidD. thymineE. ribosylthymine

30.5. 0,1,0,0,1The structural components of RNA are:A. inosineB. pseudouridineC. thymine

44

D. deoxyriboseE. adenine

31.5. 0,1,1,1,1The following chemical bonds are in the nucleic acids:A. peptide bondB. 3’,5’-phosphodiesterC. N-glycosideD. hydrophobicE. hydrogen

32.5. 0,1,1,0,1The DNA structure is:A. polyribonucleotideB. polydeoxyribonucleotideC. chain of dAMP, dGMP, dCMP, dTMPD. chain of AMP, CMP, UMP, GMPE. 5’-end is combined with phosphate

33.5. 0,0,1,1,0The confirmations for adenosine are correct:A. it has the lactam-lactim tautomerismB. it has the N1-C1-glycosidic bondC. it has the N9-C1-glycosidic bondD. it has the free amino groupsE. it doesn’t contain OH-group at C2-atom of pentose

34.5. 0,1,1,0,0The confirmations about cytosine are correct:A. it doesn’t contain the OH-group at C2-atomB. it has only the lactam formC. it has the molecular structure C9 H11O5N3D. it is a ribonucleotideE. it is a deoxyribonucleoside

45

35.5. 1,0,1,0,0The properties of nucleic acids components are:A. the nitrogenous bases (NB) are dissolved badly in waterB. the NB don’t have the lactam-lactim tautomerizmC. the nucleosides are more soluble than the corresponding basesD. purine nucleotides are more stable to heating in acidic mediumE. the purine nucleotides are more stable to hydrolysis

36.5. 0,1,1,0,0Thymine:A. is a purine nitrogenous baseB. is a pyrimidine nitrogenous baseC. has the lactam-lactim tautomerismD. has optic isomersE. is converted to hypoxanthine and xanthine

37.5. 0,1,1,0,1The quantitative determination of nucleic acids (NA) at260-280 nm is based on the:A. pyrimidine basesB. nitrogenous basesC. increasing of NA content during DNA denaturationD. phosphoric acidE. increasing of NA during acidic hydrolysis

38.5. 0,1,0,0,1The final acidic hydrolysis of nucleic acids (NA):A. the phosphodiester bonds are hydrolyzed by pyrophosphorilaseB. the phosphodiester bonds are hydrolyzed by phosphodiesterasesC. the end product is cytidineD. the end product is guanosineE. the end product is phosphoric acid

46

39.5. 0,0,0,1,0How many hydrogen bonds are there between T-C-G-A-G siteand its complementarity site of DNA?A. 10B. 11C. 15D. 13E. 17

40.5. 1,0,0,0,1According to the secondary structure of DNA, it is correct:A. it is a double helixB. the DNA chains are parallelC. it is a single chainD. the chains are combined by phosphodiester bondsE. the nitrogenous bases protrude into the interior of the helix

41.5. 1,1,0,0,1According to DNA, it is correct:A. the double-helix is a plectonemic oneB. the positions of nitrogenous bases are based on hydrophobic

interactionsC. the nucleotides of DNA-chains are similarD. the nucleotide sequence of DNA-chains are similarE. the planes of nitrogenous bases are perpendicular to axis of

helix

42.5. 1,0,1,1,0It is correct for DNA:A. the step (one full turn) of helix has 10 nucleotides and 34 AB. the parallel chains are complementaryC. the antiparallel chains are complementaryD. the various types of DNA are conditioned by dehydrotation

differenceE. the one full turn of DNA A-form contains 10 nucleotides

47

43.5. 1,1,0,0,1According to DNA, it is correct:A. one full turn of classic B-form contains 10 nucleotidesB. one full turn of A-form contains 11 nucleotidesC. the Z-form contains 12 nucleotides and is the left-spiraledD. all types of DNA have the relation C+G/A+T=1E. the complementary nitrogenous bases are: A-T and G-C

44.5. 1,0,1,0,0It is correct for DNA:A. the DNA of one species is independent on age, food and exter-

nal environmentB. all DNA have G/C=1 and G/T=1C. all DNA have A/T=1 and G/C=1D. the double-helix has the 5,4 nucleotides for one turnE. one turn of helix has 5,4 A

45.5. 0,1,1,0,0For DNA, it is correct:A. between adenine and uracil there are two hydrogen bondsB. the DNA of procaryotes is the cyclicC. DNA has structural and regulatory sitesD. the length of eucaryotes gene may be calculated according to

the number of amino acids in proteinE. the length of nucleic DNA in a cell is 2 mm

46.5 ,0,1,1,0,0For DNA, it is correct:A. the double-helix is a stable structureB. the double-helix has an essential mobilityC. the changes of the helix structure are dependent on the external

environment of DNAD. the main form of DNA is the relaxing formE. the number of DNA cycles is constant and doesn’t change

48

47.5. 1,1,0,0,0For DNA, it is correct:A. the double-helix is a high-cooperative structureB. it is denaturated in acidic or basic solutions at high temperatureC. the DNA denaturation is a irreversible processD. there is no dependence between to for DNA melting and its

nucleotide compositionE. the phosphodiester bonds breakdown during denaturation

48.5. 1,0,1,1,1For DNA, it is correct:A. the DNA is renatured at a to lower than a to for its meltingB. the DNA has the prevalence of the positive superspiralizationC. the DNA has the prevalence of negative superspiralizationD. the degree of DNA despiralization is defined by superspiraliza-

tionE. energy for DNA spiralization is proportional to square of cycles

49.5. 1,0,0,1,1Adenilic acid:A. consists of nitrogenous base, pentose and phosphateB. is a deoxyribonucleotideC. has an a-glycoside bondD. is AMPE. is cAMP

50.5. 1,1,1,0,0For nucleosome, it is correct:A. it is a repeated structural subunit of chromatinB. it is a superorganized structure of DNAC. DNA has a bond with the basic proteins-histonesD. DNA has a hydrophobic bond with proteinsE. DNA has a covalent bond with proteins

49

51.5. 1,1,1,0,0For nucleosome, it is correct:A. nucleosome includes 8 histones: H4, H3,H2a and H2bB. the DNA helix from 146 nucleotide pairs has two cycles around

octomerC. the H1-histones are bound with internucleosome siteD. it is a superorganized RNA structureE. it is an extrachromosome DNA molecule

52.5. 1,1,0,0,0For nucleosome, it is correct:A. it is a disking hertone-containing unitB. the bond between DNA and histones is ionicC. it is formed as a result of mRNA and histones interactionD. a chromatin is a composed prevalence of RNA (35%)E. ia a synonyme of polyribosomes

53.5. 1,1,0,1,0Histones:A. are constant according to the amino acid composition and ele-

ctrical chargeB. contain high amounts of lys and argC. contain high amounts of asp and glyD. the phosphorilic histones promote the transcriptionE. the histone H1 prevails in a nucleosome

54.5. 0,1,0,1,1For RNA, it is correct:A. the cellular RNA content is constantB. it is a single-stranded ribonucleotideC. it is composed of AMP, GMP, TMP, CMPD. the RNA-chain is polarE. the nucleotides are combined by 3’,5’-phospho-diester bond

50

55.5. 1,1,1,0,0For mRNA, it is correct:A. it is a geterogenic moleculeB. each gene has its mRNA moleculeC. it sintetizes and breaks very rapidlyD. contains minor basesE. permanently it is combined with ribosome

56.5. 1,0,0,1,0For mRNA, it is correct:A. it has a temporary bond with ribosomesB. it is an exact copy of the DNA chainC. the 5’-end has the poly-A sequenceD. it has an information about protein synthesisE. the relation U/A=1

57.5. 1,0,0,1,0For mRNA, it is correct:A. it transfers the genetic information from nucleus to ribosomesB. it is a double-chain polynucleotideC. the 5’-end contains the CCA sequenceD. it contains methyl-containing basesE. it has a small molecular mass

58.5. 0,1,1,0,0For mRNA, it is correct:A. it transfers the amino acids to site for protein synthesisB. mRNA molecules have the main structural peculiaritiesC. are single-chain moleculesD. are double-chain polynucleotidesE. contains only the main nitrogenous bases

59.5. 1,1,0,1,0For mRNA, it is correct:A. it has a structure of the “clover leaf”

51

B. an amino acid is composed of 3’-OH of adenine nucleotideC. an anticodon loop consists of 3 nucleotidesD. an anticodon loop consists of 7 nucleotidesE. it consists of 50-60% of RNA cell content

60.5. 0,1,1,1,0For rRNA, it is correct:A. it has the similar form and sizeB. consists of 75% of RNA cell contentC. are macromolecules with lightly changed conformationD. each type of rRNA has its space structureE. in the cell is found in free state

61.5. 1,0,0,1,1The structure and functions of ribosomes:A. the ribosomes may be reverse dissotiated to subunitsB. there are 4 centers in the ribosomesC. the subunits composition requires of extraribosome factorsD. the large subunit contains 23S and 5S rRNA, and L 1-3 proteinsE. the small subunit contains 16S rRNA and S 1-21 proteins

62.5. 0,1,1,0,1DNA replication, it is characterized by:A. a participation of corresponding nucleoside diphosphatesB. the presence of Mg2+, Mn2+, Zn2+ ionesC. a participation of deoxyribonucleotide triphosphatesD. cytoplasm is the place for DNA synthesisE. the growth chain has 5’ to 3’ direction

63.5. 1,1,0,0,1The typical characteristics of DNA biosynthesis:A. replication is a semiconservative processB. it requires the presence of double-chain mDNAC. a primer is not necessary

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D. only the deoxyribonucleoside phosphates are requiredE. the nucleus is the place for DNA synthesis

64.5. 1,0,1,1,0For replication, it is correct:A. it is based on the complementary interaction of nitrogenous

basesB. the daughter’s and mother’s chains have the identical nucleoti-

de sequenceC. replication is accompanied by despiralization of DNAD. replication goes in both directions with the same rateE. replication goes only in one direction

65.5. 1,0,1,0,1For replication, it is correct:A. the initiation of replication is conditioned by specific proteinsB. the initiation of replication is conditioned by helicase and topo-

isomeraseC. hydrolysis of pyrophosphate is the motive force of this processD. it does not need a stable proteins presenceE. the whole ribosome acts simultaneously

66.5. 1,0,1,1,1The complex of DNA-replicase of procariotes includes:A. DNA polymerases I,II,IIIB. NAD dehydrogenasesC. helicasesD. topoisomerasesE. RNA polymerases

67.5. 1,1,0,0,1The Okazaki fragments:A. these are short DNA fragmentsB. are sintetized in 5’ to 3’ direction

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C. these are noninformative DNA sitesD. are sintetized in 3’ to 5’directionE. exist for a short time period

68.5. 1,1,0,0,1The Okazaki fragments:A. a primer is necessary for the each fragmentB. are connected by the action of DNA ligasesC. are produced by RNA polymerase IID. are produced by the action of revertasesE. ATP is required for the connection of fragments

69.5. 1,0,0,1,1The DNA polymerase III:A. the template presence is necessaryB. may be the initiator of the DNA chains synthesisC. the presence of nucleoside diphosphates is requiredD. has a 3’-5’exonuclease activityE. has an editorial function

70.5. 1,1,1,0,0The DNA polymerase III:A. this is a polyenzyme complexB. it synthetizes of DNA chainC. it has sites for connection of RNA, dRTP and catalysisD. it forms of DNA chain in direction from 3’ to 5’E. the polymerization is provided by ATP hydrolysis

71.5. 0,1,1,0,1The DNA polymerase I:A. synthetizes the DNA chain de novoB. has the 5’-3’-exonuclease activity for primer removalC. has the polymerase activity for dRN addition

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D. irreversible process is based on the pyrophosphotase actionE. catalyzes the synthesis of DNA which is similar with template

72.5. 0,1,1,0,1The RNA participates in replication as:A. a substrate of DNA ligaseB. forms the phosphodiester bonds between deoxyribonucleotidesC. forms hydrogen bonds with DNA templateD. is a substrate for RNA polymerase IE. is necessary to slow the chain production

73.5. 0,1,1,1,0Transcription:A. simultaneously the whole chromosome worksB. is asymmetricalC. only certain DNA sites workD. the double-helix of DNA is templateE. template is the noncodogenic DNA chain (-)

74.5. 0,1,1,0,0For the RNA synthesis, it is correct:A. the substrates are ribonucleoside diphosphatesB. is reverseC. the Mg2+, Mn2+ presence is requiredD. both DNA chains are templateE. the cytoplasm is the site for biosynthesis

75.5. 1,1,1,0,0For the RNA synthesis, it is correct:A. the substrates are ribonucleoside diphosphatesB. the mechanism of synthesis is continuousC. the motive power of transcription is pyrophosphate hydrolysisD. the mechamisms of replication and transcription are differentE. the RNA-transcript has the equimolar quantity of A and T

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76.5. 1,0,0,1,0The procaryotes RNA polymerase:A. is a holoenzymeB. has nucleotidase propertiesC. needs a primer for synthesisD. doesn’t have the editor propertyE. translates information by a semiconservative mechanism

77.5. 0,1,1,1,0For procaryote RNA polymerase, it is correct:A. it is the pentamer of alfa2-beta2-H subunitsB. it is the pentamer of sigma-alfa2-beta2C. holoenzyme is the initiator of synthesisD. the active center has two sites for DNA and substratesE. the tetramer – alfa2-beta2 of “cor”-enzyme is the initiator of the

process

78.5. 0,0,1,1,1The common characteristics of DNA and RNA biosynthesis:A. a primer synthesisB. using the deoxyribonucleoside triphosphatesC. using the ribonucleoside triphosphatesD. the motive power of elongation is pyrophosphate hydrolysisE. the synthesis of chains goes in 5’ to 3’ direction

79.5. 1,1,1,0,0For eucaryote RNA polymerases, it is correct:A. RNAase I synthetyzes the rRNA (28S and 18S)B. RNAase II synthetyzes the mRNAC. RNAase III synthetyzes the tRNA, rRNA 5S and small mole-

culesD. dublicates the noncodogenic DNA chain in 3’ to 5’ directionE. dublicates both DNA chains in 3’ to 5’ direction

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80.5. 1,1,1,0,0For RNA polymerase, it is correct:A. sigma-subunit is activator for recognition of promotor by

RNAaseB. sigma-subunit insreases the enzyme affinity to promotorC. sigma-subunit participates in DNA double-helix despiralizationD. sigma-subunit is coordinator for elongationE. sigma-subunit combines with DNA template strongly

81.5. 1,1,1,0,0The end of transcription is conditioned by the:A. symmetrical structure of RNA-transcriptB. “ro”-proteinC. specific nucleotide sequence of the DNA chainD. RNAases activities as holoenzymeE. presence of some proteins which are combined with promotor

82.5. 0,1,1,1,0The proteinic (“ro”) r-factor:A. fixes weakly to promotorB. participates in correct termination of transcriptionC. uses the ATP for carrying out its functionD. breaks off the RNA polymerase actionE. moves with RNAase in 3’ to 5’ direction

83.5. 0,1,0,1,1The polynucleotide phosphorylase, correct answer:A. the ribonucleoside triphosphates are substratesB. the ribonucleoside diphosphates are substratesC. the DNA-template presence is neededD. may be found in bacteriaE. the polymerization may only be possible in the presence of cer-

tain mononucleotides

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84.5. 0,1,0,0,1The RNA processing is the:A. Okazaki fragments bindingB. 7’-methylguanine combines with 5’-endC. addition of CCA-sequenceD. place for processing is cytosolE. nucleus is place for processing

85.5. 1,1,1,1,0The RNA synthesis of eucaryotes:A. polyA sequence is formed by enzyme on the 3’-end of RNAB. a removal of introns takes place during processingC. the removal of introns is produced by means of nucleus RNA

of a small massD. autosplicing takes place in guanosine and Mg2+presenceE. the sinthetized RNA has genetic information on some proteins

86.5. 0,1,1,0,0Biogenesis of tRNA, correct answers:A. an active tRNA synthetizes at onceB. RNAase participates in tRNA processingC. processing includes the modifications of pentoses and nitroge-

nous basesD. the removal of exones is based on ribozome actionE. nonenzymic hydrolysis is the main in breaking of phosphodie-

ster bond

87.5. 0,1,0,1,1rRNA biosynthesis includes:A. rRNA is synthetized in cytosolB. rRNA of small molecular mass is synthetized by RNA polymerase IIC. RNA transcript goes out from cell nucleusD. after processing RNAases go out from cell nucleusE. the synthetized RNA is combined with protein (production of

ribonucleoproteinic complex)

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88.5. 0,1,0,1,1RNA-dependent RNA-polymerase:A. synthetizes in 3’ to 5’ directionB. uses the nucleoside triphosphates as substratesC. uses the RNA as templateD. present in viruses onlyE. the synthetized RNA is analogous of RNA virus

89.5. 1,0,1,1,0RNA-dependent RNA-polymerase:A. call the revertase (reverse transcriptase)B. mRNA presence is necessaryC. is synthetized of DNA on RNA templateD. uses for DNA synthesis in genetic engineeringE. promotes for RNA virus insertion to human genome

90.5. 1,1,1,1,0DNA reparation, it is correct:A. DNA-reparase (DNA-polymerase I) synthetizes the correct siteB. DNA-polymerase I uses the free 3’OH group of the interrupted

chain as primerC. repairing DNA-polymerase has the exonuclease activityD. DNA-ligase splices of DNA-endsE. DNA-glycosidases hydrolyze the 3’-5’ phosphodiester bonds

91.5. 1,1,1,0,0The reparation of thymine-dimer is:A. the presence of photoreagent enzyme – photolysisB. breakdown of covalent bondsC. including the complementary cytosine by DNA-polymerase ID. GTP energy is usedE. synthesis of a new primer

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92.5. 0,0,1,0,1In DNA reparation do not participate:A. glycosidasesB. endonucleasesC. DNA-polymerase IIID. DNA-polymerase IE. RNA-primase

93.5. 1,1,1,1,1The DNA damages may lead to:A. the amino groups lossB. formation of nonpurinic zonesC. formation of thymine dimersD. a replacement of DNA bases goes to produce mistakes during

replicationE. insertion of normal bases

94.5. 1,1,1,1,0Peculiarities of DNA replication of eucaryotes:A. DNA primer includes about 10-20 nucleotidesB. replication and synthesis of corresponding proteins go simulta-

neouslyC. the replication rate is lower than the one in procaryotesD. has many starting points for replication (replicons)E. is one-direction

95.5. 1,0,0,0,1Genetic code:A. is tripletB. is one nucleotideC. codons are read in 3’ to 5’ directionD. on mRNA the codons are divided by nonsense codonsE. code is degenerate (redundant)

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96.5. 1,0,1,0,1Genetic code: which is correct?A. is universal for procaryotes and eucaryotesB. has 3 codons for initiationC. certain amino acids have the some codonsD. has one codon for termination onlyE. has colinearity

97.5. 0,1,1,0,1Genetic code, it is correct:A. codons for one amino acid are synonymsB. codons-synonyms are nonsense triplets for amino acidsC. nonsense codons are signals for termination of protein synthe-

sisD. nonsense codons are noncorresponding diplets for amino acidsE. one codon can’t be a sense codon for one amino acid

98.5. 0,1,0,1,1Codon AUG:A. is the codon for cysteineB. is the initial codon for translationC. is the initial codon for transcriptionD. is the codon for methionineE. is the codon for formyl-methionine

99.5. 1,1,1,0,0Genetic code, it is correct:A. the chemical peculiarities of certain amino acids are reflected

by codon structureB. for codons-synonyms which have the difference of first or

second codons different tRNAs are requiredC. anticodons with inosine on the first position for three codons

are corresponded

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D. anticodons which have A or C on the first position correspondfor two codons

E. anticodons which have U or G on the first position correspondfor one codon

100.5. 0,1,1,0,1Introns:A. they are on the mature mRNAB. they are on the same sites of the related genesC. their removal is regulated of mRNA transport from nucleusD. their removal is a posttranscriptional processE. are the result of a corresponding gene evolution

101.5. 1,0,0,1,1The effect of nitric acid (HNO2) on genome is produced by:A. convertion of adenine to hypoxanthineB. insertion of one base pairC. deletion of one base pairD. convertion of cytosine to uracilE. replacement of the base pair G-C by A-T

102.5. 1,0,0,0,1The “point” mutations:A. are based on the chemical change of one base of one DNA chainB. all codons of defective DNA are changed as a result of transi-

tionC. all codons of defective DNA are changed as a result of trans-

vertionD. are based on the chemical changes of the both complementarity

basesE. are based on the change of one codon

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103.5. 0,1,0,0,1The transversion mutation is:A. replacement of one base by another baseB. replacement of one stop-codon by the sense codonC. replacement of sense codon by the nonsense codonD. alterations of all codons as the result of mutationsE. replacement of pyrimidine base by purine base

104.5. 0,1,0,0,1Mutation is the result of deletion in case of:A. replacement of certain purine bases by pyrimidine basesB. alteration of all codons as a result of mutationC. is the result of buildingD. is caused by structural analogs of nitrogenous basesE. replacement of one sense codon by the nonsense codon

105.5. 0,0,1,1,0Mutations don’t lead to disturbances:A. between exon-intronB. “pointing” on intronsC. reverse to normal codeD. which are formed by codons-synonymsE. the “pointing” for amino acids on a special side of protein

106.5. 1,1,1,1,1Consequences of mutations:A. cessation (stop) of polypeptide chain synthesisB. synthesis of the additional polypeptide chainC. synthesis of the changed DNA moleculesD. formation of the abnormal proteinsE. some mutations don’t change the amino acids sequence

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107.5. 0,1,1,1,0Enzymes for restriction:A. act on mRNAB. they are in bacterial cellsC. breakdown the double helix of DNA with double-direction

symmetryD. are the endonucleases which recognize and restrict of polyn-

drome sequencesE. act on one chain of DNA

108.5. 1,0,1,0,1Enzymes for restriction:A. breakdown one phosphoester bond on both chains of DNAB. can break the polydeoxy-RNA according to the scheme:

C-C-A-/-T-G-G-C-C-C. they are in bacteria onlyD. break the poly-RNA chain according to the scheme:

C-U-U-/-A-U-U-C-E. participate in the formation of molecular clone in genetic en-

gineering

109.5. 1,1,0,0,1Plasmids:A. are replicated autonomically and quicklyB. are used as vector for gene inculcationC. have the template of DNAD. are large molecules which can’t penetrate the host cell mem-

braneE. are in bacterial cell only

110.5. 0,1,1,0,1This confirmation for plasmids is correct:A. don’t have the quality of autoreplicationB. can be substrates for restriction’s enzymes

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C. are small molecules which can penetrate the host cell membraneD. plasmid’s DNA with specific proteins present in nucleosomeE. plasmid’s DNA is in cytosol in most of bacteria

111.5. 1,1,1,1,1Genetic engineering includes the following manipulations:A. cloning DNA and plasmid breakdown by action of restriction’s

enzymeB. selection of cells, which have plasmidsC. insertion of recombinant DNA in plasmids with help of DNA-

ligasesD. multiplication of plasmids at the same time with bacteria repro-

duction (amplification of introduced genes)E. introduction of vector to bacteria cell

112.5. 0,0,1,0,0Show the sequence of processes for genetic recombination,types and necessary enzymes: 1-lysogenya, end transferase; 2-transduction, restricting enzymes; 3-conjugation, transferase;4- transformation, reverse transcriptase.A. 1-2-3-4B. 2-1-4-3C. 4-2-3-1D. 4-1-2-3E. 3-1-2-4

113.5. 1,1,0,0,1According to aminoacyl-mRNA synthetases, it is correct:A. specificity is defined by the t-RNA structure onlyB. exactness is provided by ability for autocontrolC. protein composition defines of enzyme specificityD. exactness doesn’t depend on enzymesE. has free SH-groups

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114.5. 1,0,0,1,0For activation of amino acids, it is correct:A. the place of amino acids activation is cytosolB. process has 5 stepsC. for each of amino acids there is one specific tRNAD. for activation of amino acids an energy of 2 macroergic bonds

is necessaryE. a complex of amino acid-tRNA is formed at the level of ribo-

somes

115.5. 1,1,0,0,1Formation of amino acid-tRNA complex (AA-tRNA):A. the bond between AA-tRNA is macroergicB. action of pyrophosphatases stipulate unreversible reactionsC. AA combines with tRNA by amid bondD. activation of all AA is catalized by 64 AA-tRNA synthetasesE. activation of all AA is catalized by 20 AA-tRNA synthetases

116.5. 1,1,0,1,0Initiation of protein synthesis requires:A. the whole ribosomeB. m-RNAC. peptidyl transferaseD. GTPE. arginine

117.5. 1,1,0,0,1Complex for initiation of protein synthesis includes:A. functionaly active ribosome 70SB. mRNA with codon AUG on the A-siteC. mRNA with codon AUG on the P-siteD. N-formylmethionyl-tRNA (fmet) on A-siteE. factors of initiation: IF1, IF2, IF3

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118.5. 0,1,0,1,1According translation is correct:A. synthesis of polypeptide chain starts on the C-endB. synthesis of polypeptide chain starts on the N-endC. initiative amino acid for procaryotes is methionineD. donor of formyl is the N10-formyl-FH4E. formation of formyl-tRNA is catalized by specific transformylase

119.3. 0,0,1Show the sequence of steps for initiation of protein synthesis:1 - release of initiation factors and GTP hydrolysis; 2 – disso-ciation of 70S ribosome on the subunits; 3 - joining the IF3 to30S subunit; 4 - joining the tRNA to 30S subunit; 5 - joiningthe N-formylmet-tRNA (fmet)-IF2-GTP to the previous complex;6 - joining the end complex to 50S subunit.A. 1-3-6-4-5-2B. 3-5-4-1-2-6C. 2-3-4-5-6-1

120.5. 1,0,0,1,1Elongation of protein synthesis is needed:A. initiation complexB. aminoacyl-tRNA synthetaseC. ATPD. peptidyl transferaseE. Tu, Ts, G factors

121.5. 1,0,1,0,1During protein biosynthesis for elongation is characterized:A. formation of peptide bondsB. connection of formylmet-tRNA on the P siteC. using the 2 GTP moleculesD. formation the peptide bond between amino group of the P-cen-

ter and carboxylic group of the A-centerE. ribosome’s moving on one codon of mRNA

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122.5. 1,1,0,0,0Elongation of protein biosynthesis is included:A. connection of mRNA and the second amino acid on A centerB. formation of the peptide bond between COOH of the P-center

and NH2 of the A- centerC. dissociation of ribosome on subunitsD. separation of protein from ribosomeE. using the 2 ATP molecules and Ca2+iones

123.3. 0,1,0Put the elongation steps of protein synthesis in succession:1 - complex AA-tRNA-Tu-GTP combines to initiation complex;2 - transference of dipeptide is needed Od TF-G and 1 GTPmolecule; 3 – hydrolysis of GTP; 4 - Tu-GDP goes out the ri-bosome and composes the Ts-GTP ; 5 - transport of ribosomeon one triplet of mRNA; 6 - transport of formylmethioninefrom P-site to A- site with production of dipeptide-mRNA;7 - the free mRNA goes to cytosol after hydrolysis.A. 1-7-2-6-3-5-4B. 1-3-4-6-5-7-2C. 3-7-2-4-5-6-1

124.3. 1,0,0Put the transcription steps in succession: 1 - growth of RNAchain with help of corenzyme, with moves in 3’ to 5’ directionof DNA; 2 - joining of gene with RNA polymerase with help ofsigma-subunit; 3 - processing of RNA; 4 - untwisting of theDNA duble helix, synthesis and formation of phosphodiesterbonds; 5 - recognition of RNA polymerase one of the promo-tor’s sequence; 6 - r-factor stops the RNA synthesis; 7 - sigma-subunit is dissotiated by action of holoenzyme.A. 5-2-4-7-1-6-3B. 3-7-2-4-5-6-1C. 1-3-2-4-7-5-6

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125.5. 1,0,1,1,0During termination of protein synthesis takes place:A. Release on the end mRNA from the P-siteB. using of the 3 ATP moleculesC. release of the synthetized protein by hydrolysisD. dissociation of ribosome on it’s subunitsE. reading the all stop codons

126.5. 1,1,0,1,0According to the termination of protein biosynthesis the con-firmations are correct:A. is needed of the factors R1, R2, SB. mRNA is releasedC. is needed the presence of factor FD. is needed of GTP usingE. the last complex AA-mRNA is hydrolized by termination factor

127.5. 1,0,1,1,0Posttranslational modifications include:A. production of hydroxyproline from prolineB. splicing of intronsC. acetylation of N-endD. methylation of lysine, arginineE. production of polyadenilate

128.5. 1,1,0,0,1Posttranslation modifications include:A. release of some polypeptide sitesB. joining the nonproteinic groups (heme)C. replacement of the purine bases by the pyrimidine onesD. formation of the hydrogen bonds in the structure (a-helix)E. carboxylation of glutamate

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129.5. 1,0,1,0,1The processes which are needed for the 1 GTP molecule using:A. combining of the arginine mRNA on the A-center of ribosomeB. activation of methionine by methionine-mRNA synthetaseC. transport of peptidyl-mRNA from A-center to P-centerD. joining the mRNA to the small of subunitE. activation of the alongation Tu factor

130.5. 1,0,0,1,1Choose of the protein biosynthesis inhibitor for the replication:A. streptomycinB. erythromycinC. puromycinD. mitomycin CE. canamycin

131.5. 1,0,0,1,0Choose the inhibitors for transcription:A. amanitinB. actinomycinC. penicyllinD. rifamycinE. erythromycin

132.5. 1,0,0,1,0Choose the inhibitors for translation:A. tetracyclineB. aminicinC. actinomycinD. puromycinE. streptomycin

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133.5. 1,0,0,1,1Protein biosynthesis is regulated by:A. equilibrium between production and breakdown of mRNAB. synthesis rate of mRNAC. breakdown rate of mRNAD. quantity of mRNAE. expression of corresponding genes

134.5. 1,1,0,1,0mRNA stability:A. based on the complex structureB. is increased without 5’-segmentC. is increased in the presence of 5’-segmentD. the presence on 3’-fragment of U and A is increased in its hy-

drolysisE. stability is decreased by action of estrogenes, GTH

135.5. 1,0,1,0,0mRNA stability, correct:A. cell RNA is destroyed by viruses actionB. cortisol decreases the mRNA stabilityC. estrogenes increase the mRNA stabilityD. mRNA breakdown rate doesn’t depend on its structureE. mRNA breakdown rate is dependent on rRNA

136.5. 0,1,0,0,1Regulation of the anabolic vital cell processes is dependent on:A. presence of inductive enzymesB. presence of repressory enzymesC. presence of the constitutive enzymesD. coordinative inductionE. coordinative repression

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137.5. 1,0,1,1,0Protein biosynthesis regulation:A. is dependent on regulative nucleotidic sequences enhancers (E)

and silancers (S)B. activities of E and S don’t depend on hormonesC. is dependent on symmetrical complex of proteins, E and SD. among the combined DNA proteins is a different correlationE. doesn’t depend on rRNA proteins action

138.5. 0,1,1,0,0For lag-operon theory is correct:A. cAMP concentration is increased according to the glucose con-

centration riseB. CAP has the two centers for connection of cAMP and DNAC. repressor has two centers for connection of inductor and fixa-

tion on operatorD. LAC genes are transctipted in/or without presence of lactoseE. LAC genes are transcripted independently in connection with

repressor and operator

139.5. 1,1,0,0,1For LAC operon theory is correct:A. activation of LAC operon goes without glucoseB. regulatory genes are codons for repressor, which fixes gene

operatorC. glucose is the inductorD. inductor fixes the promotorE. repressor-inductor complex promotes for connection of pDNA

with promotor

140.5. 1,0,0,1,1Regulation of the genetic expression:A. lactose decreases affinity of repressor to operatorB. lactose metabolism is regulated by CAP-cAMP complex only

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C. lactose metabolism is regulated by repressor-inductor complexonly

D. corepressor increases the repressor affinity to operatorE. lactose metabolism is regulated by two mechanisms (CAP-

cAMP, repressor-inductor)

141.5. 1,0,1,1,0Regulation of genetic expression:A. enhancers-sites are positive regulators for protein synthesisB. enhancers have the species specificityC. the enhancers ends aren’t correct and have conservative zonesD. enhancers have the expressed tissue specificityE. the enhancers position according to the gene doesn’t change

142.5. 1,0,1,1,0Induction and repression of enzymes:A. induction is determined the “de novo” synthesis of the enzymic

moleculesB. repression is analog of retroinhibitionC. repression and induction are based on the economic principle

in the cellD. repression is the inhibition of enzyme synthesisE. induction doesn’t define the new synthesis of enzyme molecules

143.5. 1,1,1,1,0Replication, the correct confirmations:A. DNA polymerase combines the nucleotides to 3’-growth chain

onlyB. 3’-end of the mature chain isn’t replicatedC. 5’-end of the daughter chain is shortD. 3’-end of the mature chain is freeE. it is the incomplete replication of growth chain

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144.5. 1,1,1,1,0According to the telomerase, it is correct:A. takes place the DNA shortening for the majority of somatic

cellsB. the DNA shortening doesn’t meet in the sexual and tumor cellsC. the DNA shortening is prevented by telomeraseD. enzyme which is prevented by DNA shortening is transferaseE. isn’t reverse transcriptase (revertase)

145.5. 0,1,1,0,1Telomerase:A. ribonucleotideB. ribonucleoproteinC. enzyme for compensation of replication endD. enzyme, which uses the ribonucleotidesE. enzyme, which uses the deoxyribonucleotides

146.5. 1,1,1,0,1Telomerase:A. has the proteic component TPTB. TPT is universal for eukaryotesC. enzyme acts as the stable nucleoproteinic complexD. hasn’t the distinctive properties with reverse transcriptases (re-

vertases)E. the small proteins participate in regulation of enzyme action

147.5. 0,1,0,1,0Chromosome elongation of eucaryotes:A. combines the hexonucleotide TTAGGGB. 3’-end of DNA is extended of hexonucleotide TTAGGGC. 5’-end of DNA is extended that nucleotideD. in succession goes: fixation, elongation and translocation of te-

lomeraseE. at first is extended by the opposite daughter chain (C)

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148.5. 0,1,1,0,1Enzymic characteristics for telomerases:A. enzyme has the small activity “in vitro”B. the human enzyme has high activityC. process is dependent on the length primerD. the primers are smaller than 10 nucleotidesE. when the primer is more than 10 nucleotides the DNA can have

the thousands of nucleotides

149.5. 1,1,0,0,1Enzymic characteristics of telomerases:A. they use deoxynucleotides for chain synthesisB. RNA-RNA as substrate may be usedC. they use dideoxynucleotide TP for elongationD. K+ and Na+ are needed for their functionE. they have exonuclease activity

150.5. 0,1,1,1,0Structure and functions of RNA telomerase:A. RNA structure of the related organisms is very conservativeB. the primary structure has difference of sequence and nucleoti-

de’s numberC. messenger site is on 50N of the 5’-endD. secondary structure includes 4 parts and one chain fragmentE. RNA telomerase isn’t used for enzyme catalysis

151.5. 1,1,1,0,1Proteins of telomerase complex:A. haven’t homologic primary structureB. are similar with RNA polymerasesC. the functional spectrum of these proteins is very variableD. RNA telomerase hasn’t equimolar quantity of p80 and p95E. polyproteinic complexes at the action with DNA are genes re-

pressors

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152.5. 1,1,1,0,0Regulation of telomerase activity in somatic cells:A. cytokines are activators of telomeraseB. takes place in the autoinduction of proliferation, autorestora-

tionC. in endometric cells of uterus is depended on mensus cycleD. after menopause activity of telomerase is increasedE. estrogenes are inhibitors of it’s activity

153.5. 1,0,1,1,0Activators and inhibitors of telomerase:A. azidothymine is its inhibitorB. dideoxyguanosine is modern activatorC. as inhibitor isn’t DNA corresponding telo-RNAD. may be used as regulators of reverse transcriptasesE. the complementary for matrix telo-RNA olygonucleotides are

activators

154.5. 1,1,0,0,1The correct confirmations:A. a loss of telomerase’s properties is a reason for ageingB. the telomerase length is biological age for growing oldC. replicative folk is into cell cytosolD. problem of incomplete replication is specific for cyclic DNAE. telomerase has thousands of TTAGGG sequences

155.5. 1,1,0,1,1The correct confirmations:A. with age the oxygen active forms (OAF) are depositedB. the old age is the phenomen of phenoptosisC. OAF have the ptotective function for living systems (cell, my-

tochondria)D. superoxide anion radical (:O2-) is initiator of OAF productionE. mytochondria have the special role for OAF generation

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156.5. 1,1,1,1,1Mechanisms of the growing old organism:A. production of anomalic chromosome is increasedB. chromosomes loss are predominatedC. takes place the gene extraction near telomeraseD. after extraction of this gene the growing old repressor is inacti-

vatedE. the telomer binding proteins (TBP) are included in process

157.5. 1,1,0,1,1The cell growing old is based on:A. activity of cGMP dependent protease is increasedB. activation of genes for protein phosphorylationC. loss of the proteins-repressors for telomerase geneD. presence of the prohimbitine geneE. activation of methylguanine transferase

158.5. 1,1,1,1,1It is correct:A. 5’-methylcytosine number is needed for immortal fenotypeB. the mortalin present in the cytoplasm of normal human cellsC. a quarter of all immortal cells are telomer-negativeD. the telomerase length may be constant by recombination and

retrotranspositionE. the cells have an alternative mechanisms for telomer lengthe-

ning

METABOLISM. BIOLOGICAL OXIDATION. RESPIRATORYCHAIN

1.5. 1,1,0,1,1The functions of metabolism are the following:A. to supply the cells with chemical energyB. transformation of nutritious substances into building blocks

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C. synthesis only specific biomoleculesD. catabolism of specific biomoleculesE. assembling of polysaccharides and other cell components

2.5. 0,1,1,0,1The following statements are correct:A. catabolism is a stage of degradation of only exogenous substan-

cesB. catabolism is a stage of degradation of various substances to

more simple onesC. catabolic processes are accompanied by release of free energyD. the energy is collected only as ATPE. the energy may be collected both as ATP and GTP

3.5. 1,1,0,1,0The following statements are correct:A. anabolism is a stage of synthesis of various organic compoundsB. anabolism consumes free energy (ATP)C. anabolism requires hydrogen atoms delivered by NADНD. anabolism has 3 stagesE. for anabolism is characteristic a convergence of metabolic path-

ways

4.5. 0,0,1,1,1The following statements are correct:A. catabolic and anabolic pathways have the same directionB. the speed of catabolic and anabolic pathways is regulated by

common enzymesC. catabolic and anabolic pathways differ in localizationD. catabolic and anabolic pathways have a common third stageE. reactions of catabolic and anabolic pathways should be regu-

lated separately

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5.5. 0,1,1,0,1Cycle ATP:A. ATP – is the main form of chemical energy storageB. in all living cells carries out identical functionsC. it is the universal and main carrier of energyD. ATP is presented only in mitochondriaE. in some biosynthetic reactions is used such as CTP, GTP, UTP

6.5. 0,0,1,1,1The regulation of cell metabolism:A. ADP and AMP serve as allosteric inhibitorsB. ATP serves as an activatorC. the rate of the metabolism depends on the cell needs for ATPD. the rate of the metabolism depends on the ratio NADPH/NADPE. depends on hormones

7.5. 1,1,1,0,0Which compounds are macroergic?A. ADPB. ATPC. creatine phosphateD. diacylglycerol phosphateE. glucose-6-phosphate

8.5. 1,1,0,0,1The regulation of pyruvate dehydrogenase complex:A. is carried out by retroinhibitionB. acetyl-ScoA and NADH serve as inhibitorsC. NADH is inhibitor for E2D. acetyl-ScoA is inhibitor for E3E. the allosteric inhibition is amplified by macromolecular fatty

acids

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9.5. 1,0,1,0,0The Krebs cycle:A. is a general final pathway of substances’ oxidation in living

cellsB. all compounds include in the Krebs cycle through acetyl-coAC. in the Krebs cycle Н+ and СО2 form from acetyl-coAD. for reactions of the Krebs cycle are needed the anaerobic condi-

tionsE. oxygen participates directly in the reactions of the Krebs cycle

10.5. 1,0,0,0,0Properties of a-ketoglutarate dehydrogenase complex (a-KGDHcomplex):A. derivatives of vitamins B1, B2, PP, HS-coA, lipoic acid are

includeed as coenzymeB. a-KGDH complex is regulated by both covalent modification

and allostericallyC. it has a completely different action in comparison with pyruvate

dehydrogenase complexD. NADH and succinyl-coA intensify the activity of the a-KGDH

complexE. the activity of a-KGDH complex is reduced by the low level of

cell energetic status

11.5. 1,0,1,1,0Oxidation of succinate (the 6th reaction of the Krebs cycle):A. succinate oxidizes to fumarate by dehydrogenationB. the reaction is catalyzed by NAD-dependent succinate dehydro-

genase (SDH)C. SDH is an integrated membrane proteinD. FAD is connected by a covalent bond with histidine in the acti-

ve center of SDHE. FADH2 dissociates from SDH and the electrons are transferred

to Fe3+

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12.5. 0,1,0,0,1The Krebs cycle:A. in one turn of the Krebs cycle is accompanied by formation of 3

molecules of CO2B. in one turn of the Krebs cycle only one acetyl radical is includedC. oxygen participates directly in the Krebs cycleD. for the Krebs cycle are needed only the anaerobic conditionsE. the Krebs cycle provides regeneration of 1 molecule of oxaloa-

cetate

13.5. 0,0,0,1,0The transformation of 1 molecule of isocitrate to succinate inthe Krebs cycle provides the synthesis of ATP:A. 10 moleculesB. 12 moleculesC. 8 moleculesD. 7 moleculesE. 9 molecules

14.5. 0,1,1,1,0Pyruvate carboxylase reaction:A. the reaction takes place in cytosolB. it is an anaplerotic reactionC. the reaction takes place in mitochondriaD. it is a reaction of gluconeogenesis (from alanine to glucose)E. does not require ions Mg2+ or ATP

15.5. 1,0,0,1,1Biological oxidation – the essence of process:A. it is the totality of oxidative and reductive processes that takeplace in the cellsB. occurs by addition of oxygenC. the transfer of electrons is realized directly to oxygenD. the oxidation is carried out by dehydrogenationE. the Н-atoms are transferred as protons and electrons

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16.5. 1,1,0,1,0,The correct statements about the acceptors of Н+ and ē:A. the acceptors of Н+ and ē are coenzymes of dehydrogenasesB. the electrons are the main source of energy in ATP synthesisC. NADН serves as an acceptor of electrons in reactions of biosyn-

thesisD. NADPН serves as a donor of electrons in reaction of biosynthe-

sisE. FADH2 is a donor of electrons in biosynthesis

17.5. 1,1,0,0,1Oxidative phosphorylation:A. the transfer of electrons through respiratory chain is connected

with the ATP synthesisB. delta G of two electrons is equal to 52,6 kcalC. delta G of two electrons is enough to synthesize 5 molecules of

ATPD. delta G of two electrons is enough to synthesize 1 molecule of

ATPE. the synthesis of one molecule of ATP is required a Eo = 0,224v

18.5. 1,1,1,0,1The final products of electron transfer are:A. the addition to О2 of 2 electrons forms H2O2B. the addition to О2 of 4 electrons forms 2 H2OC. the addition to О2 of 1 electron forms superoxid radical (:O2 -)D. the transfer of 2 electrons through the complex II can form 3

molecules of ATPE. the transfer of 2 electrons through the complex IV can form 1

molecule of ATP

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19.5. 1,1,1,0,0Mechanisms of oxidative phosphorylation:A. the Н-ions come back to mitochondria through the special ion

channelsB. the flow of protons is driving force, which promotes synthesis

of ATPC. ATP- syntase consists of the factors F0 and F1D. both factors are components of the inner mitochondrial mem-

braneE. ATP- syntase consists of 9 units of 5 different kinds

20.5. 1,1,1,0,1The control of oxidative phosphorylation:A. the P/O ratio is characteristics of the oxidative phosphorylationB. P/O ratio represents the number of inorganic phosphate moles,

transformed in the organic form at the utilization of 1 atom ofoxygen

C. P/O for malate oxidation is equal to 3/1D. P/O for succinate oxidation is equal to 4/1E. as uncouplers can serve hydrazones, isothiocyanates

21.5. 1,1,0,1,1The functions of metabolism are the following:A. to supply the cells with chemical energyB. transformation of nutritious substances into building blocksC. synthesis of only specific biomoleculesD. catabolism of specific biomoleculesE. assembling of polysaccharides and others cell components

22.5. 0,1,1,0,0The following confirmations are correct:A. catabolism is process only of exogenic substances breakdownB. catabolism is process of different substances breakdown to more

simple products

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C. a free energy releases during catabolismD. released energy uses only for ATP productionE. catabolism has 2 stages

23.5. 1,0,1,0,0The following statements are correct:A. intracellular anabolism and catabolism go in timeB. dosn’t release a free energy on the first stage of catabolismC. pyruvate is the end product of the 2-nd stage of catabolismD. lactate is the end product of the 2-nd stage of catabolismE. the 2-nd stage of catabolism includes the Krebs cycle

24.5. 1,1,0,1,0Characteristics for metabolism are:A. anabolic pathways are needed in additional energyB. anabolism and catabolism have common sitesC. anabolism and catabolism don’t have common sitesD. the great portion of energy is prodused on the 3-rd stage of

catabolismE. pyruvate is the end product of metabolism

25.5. 0,1,0,1,0ATP:A. is nucleotide with one macroergic (energy-rich) chemical bondB. is purinic nucleotideC. is pyrimidinic nucleotideD. has 2 macroergic bondsE. has 3 macroergic bonds

26.5. 1,0,0,0,1Which substances are more energy-rich than ATP?A. creatinphosphateB. glucose-5-phosphateC. AMPD. pyrophosphateE. phosphoenolpyruvate

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27.5. 0,0,1,1,0Pyruvate dehydrogenase complex:A. includes 48 polypeptidic chainsB. includes enzymes: E1, E2, E3, E4C. includes enzymes: E1, E2, E3D. includes coenzymes: NAD, FAD, TDP (TPP)E. includes active forms of vitamines: B1, B2, PP, B6

28.5. 0,0,1,1,0Pyruvаte dehydrogenase (PDH) complex functions are:A. pyruvate is oxidized by O2B. oxidative decarboxylation of CH3-COOHC. oxidative decarboxylation of CH3-CO-COOHD. production of NADH2 for respiratory chainE. production of NADPH2 for respiratory chain

29.5. 1,0,1,1,0The 3-rd chemical reaction of PDH complex is:A. acyl-radical transfers on HS-coA with production acyl-ScoAB. E1 is catalyst of this reactionC. E2 is catalyst of this reactionD. acyl-coA is macroergic complexE. E3 is catalyst of this chemical reaction

30.5. 1,1,1,0,0Pyruvate dehydrogenase complex regulation:A. nucleotides are regulatorsB. ATP and GTP are inhibitorsC. AMP is activatorD. only allosteric regulationE. only covalent modification

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31.5. 1,0,1,1,0The Krebs cycle, its regulative reactions and enzymes:A. citrate synthesis citrate synthetaseB. citrate isomerization aconitaseC. oxaloacetate production MDHD. succinate oxidation SDHE. malate production MDH

32.5. 1,1,1,0,0Correct statements about oxidation of succinate to fumarate:A. is needed of FADB. is needed of the active form (coenzyme) of vitamine B2C. is reaction of dehydrogenationD. is reaction of isomerizationE. is reaction of hydrotation

33.5. 0,0,0,1,0Substrate phosphorylation in the Krebs cycle:A. citrateà isocitrateB. isocitrateà a-ketoglutarateC. a-ketoglutarateà succinyl-ScoAD. succinyl-ScoAà succinateE. succinateà fumarate

34.5. 1,0,0,0,1Respiratory chain (RC):A. its components are donors and acceptors of electronsB. this is chain only of coenzymesC. this is chain only of proteinsD. RC has 4 points for phosphorylationE. RC has 3 cites for phosphorylation

35.5. 1,1,1,1,0Reactions of electron transport:A. Fe2++ Cu2+ « Fe3++ Cu+

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B. AH2 + Bà A + BH2C. donorà ē + AD. donor and acceptor are redox-pairE. donor is oxidant, acceptor is reductant

36.5. 1,0,1,1,0Complex II (succinate-coQ-reductase):A. glycerol-3-phosphate is donor of H+ and ēB. includes FMNC. has FeS-centersD. transports of H+ and ē to ubiqunonE. transports of H+ and ē to cytochrom c

37.5. 1,1,1,0,0Complex IV of Respiratory chain:A. is called as cytochrom c oxidaseB. transfers of H+ and ē to O2C. is complex for both respiratory chains, a long and short onesD. all cytochromes have a relative proteinic portionE. all cytochromes have a relative prostethic portion

38.5. 0,1,0,1,0Respiratory chain:A. FeS-proteins are cariers of H+

B. FeS-proteins are cariers of H+ and ēC. a long respiratory chain generates 4 ATP moleculesD. cytochromes are cariers only for electronsE. cytochromes are cariers of H+ and electrons

39.5. 0,1,1,1,1Respiratory chain:A. all cytochromes contain of copper (Cu)B. all cytochromes are heme proteinsC. 4 electrons are needed for reduction of O2D. Eo of ubiqinon is + 0,04 vE. cytochromes contain Fe or Cu

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40.5. 0,1,1,1,1Transport via the mitochondric membrane:A. mitochondric membrane is permiable for NAD and NADHB. protons and electrons transfer via its membraneC. malate is carier of protons and electronsD. glycerol-3-phosphate is carier of H+ and ēE. shuttle mechanisms regulate NAD+ concentration in cytosol

41.5. 1,1,1,0,1Coefficient P/O:A. for malate is 3B. for succinate is 2C. for ascorbate is 1D. for isocitrate is 2E. for isocitrate is 3

42.5. 1,1,1,0,0Cytochrom P450:A. uses O2 and COB. catalyzes reaction of substrate hydroxylationC. uses NADH and NADPHD. doesn’t participate in steroids’ synthesisE. doesn’t participate in drugs’ biotransformation

CARBOHYDRATES: CHEMICAL STRUCTURE ANDMETABOLISM

1.5. 1,1,1,0,0Name of the carbohydrate functions:A. energeticB. they are the main components of cell membranesC. geneticD. stabilize an oncotic pressureE. are emulgators

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2.5. 0,0,0,1,1In the human organism present the following carbohydrates:A. starchB. celluloseC. amylaseD. glucoseE. glycogen

3.5. 0,1,1,1,0Lactose is:A. carborydrate which has the reduce property and 2 molecules of

b-galactoseB. the mammalia milkC. disaccharide with reduce propertyD. both of its monosaccharides have the pyranose formE. repeated structural subunit of glycogen

4.5. 1,0,1,0, 1Which of these confirmations according to glucose are correct?A. may be in a- and b-form of stereoisomersB. the glucofuranose form is stableC. glucuronic acid is the product of glucose oxidationD. doesn’t have the hiral carbon atomsE. is the aldohexose with the 4 hiral carbon atoms

5.5. 1,0,1,0,0Deoxyribose:A. is the component of certain nucleotidesB. is the component of mRNAC. is the modificated aldopentoseD. can’t be as the furanose formE. has the NH-group in the site of OH-group

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6.5. 0,1,1,0,0Name the homopolysaccharides:A. heparinB. starchC. glycogenD. chondroitin sulphateE. heparan sulphate

7.5. 0,1,0,1,1Name the heteropolysaccharides:A. amylopectinB. hyaluronic acidC. maltoseD. keratan sulphateE. heparin

8.5. 1,0,1,1,1For glucose absorbtion is needed:A. Na+-ions for production complex with monosaccharidesB. abundance of Ca2+-ionesC. participation of Na+ ,K+ -ATP-aseD. a coupling of oxidative phosphorylation in enterocytesE. presence of ATP and corresponding transport mechanism

9.5. 0,1,1,1,0Breakdown of glucose into two trioses is correct:A. the end reaction is production of two aldosesB. equilibrium of this reaction goes to C=O productionC. one aldose and one ketose produce in these reactionsD. 2 molecules of ATP are as the result of the five reactionsE. all reactions of this step are indirect

10.5. 1,0,1,1,0Oxidation of glyceraldehyde-3-phosphate:A. is catalyzed by corresponding dehydrogenaseB. is irreversible

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C. is reversibleD. produces energy (ATP)E. goes in mitochondria

11.5. 0,0,1,1,0The end products of anaerobic glycolysis are:A. pyruvateB. glucoseC. 2 ATPD. 2 H2OE. 2 CO2

12.5. 1,1,1,0,0According to pentose-phosphate oxidation of glucose the con-firmations are correct:A. glucose-6-phosphate + NADP+à 6-phosphogluconate lacton +

NADP + H+

B. reaction is catalyzed by NADP-dependent dehydrogenaseC. lactonase catalyzes 6-phosphogluconate productionD. lactonase is oxidoreductaseE. 6-phosphogluconate + NADP+à ribose-5-phosphate + CO2 +

NADP + H+

13.5. 1,0,1,0,0End products of one glucose molecule oxidation are:A. 38 ATPB. 54 H2OC. 6 CO2D. 22 H2OE. 44 ATP

14.5. 1,0,1,0,1Substrate for gluconeogenesis is:A. glycerolB. acetyl-coA

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C. glutamateD. acetoacetateE. asparagine

15.5. 1,1,1,0,0Hyperglycemia may be in:A. diabetes mellitusB. pathology of cortex of medulla glandsC. using the b-blockatorD. hypothyrosisE. Addison’s disease

16.5. 1,1,0,1,0Confirmations for maltose are correct:A. it is product of enzymic hydrolysis of starchB. it is product of enzymic hydrolysis of glycogenC. it is cellulose monomerD. it is composed of two a-glucose moleculesE. it doesn’t have mutorotation property

17.5. 1,0,0,1,0Galactose is:A. lactose monomerB. the main carbohydrate of bloodC. keto-pentoseD. epimer of glucoseE. a-anomer in the structure of lactose

18.5. 0,0,1,0,0Fructose is:A. reduced only to D-sorbitolB. ketose with L-stereoformC. galactose isomerD. the main carbohydrate of bloodE. the main component of lactose

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19.5. 1,0,1,0,0Homopolysaccharides:A. are cellulose, starch and hitinB. maltose is structural subunit of celluloseC. cellulose is polysaccharide of plantD. cellobiose has 2 molecules of a-glucoseE. cellobiose has a-glycoside bond

20.5. 0,1,0,0,1Statements about glycogenolysis are correct:A. this is hydrolysis of glycogenB. phosphorolysis of glycogen is the main process in organismC. a-1,6-glycoside bonds of glycogen are broken by o-phosphate

(orto-phosphate)D. only glycogen phosphorylase is neededE. a-1,6-bonds are broken by hydrolytic enzyme

21.5. 0,1,0,0,1According to glycogenesis the following confirmations are cor-rect:A. it is active process in the cardiac muscle and nerve (brain) tissueB. it is more active in the liver and skeletal muscleC. in glycogenesis the “a” and “b” glycogen synthetases participateD. glycogen synthesis is needed of enzymic complexE. 3 of macroergic molecules are necessary for glycogen synthesis

22.5. 1,1,0,1,0For Girke disease the following confirmations are correct:A. deficiency of glucose-6-phosphatase is the reason of this patho-

logyB. lactate and pyruvate are increased in the bloodC. glycogen structure is anomalicD. the metabolic disturbances takes place in the liver, kidney and

intestineE. the reserve of glycogen is minimum

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23.5. 0,0,1,1,1Enzyme for regulation of glycolysis is:A. triose-phosphate isomeraseB. phospho-glucose isomeraseC. hexokinaseD. phosphofructokinaseE. pyruvate kinase

24.5. 0,0,1,1,1Glycolysis activator is:A. NADHB. ATPC. adrenalinD. fructose-1,6-biphosphateE. AMP or ADP

25.5. 0,0,0,1,1Inhibitor of glycolysis is:A. NADB. citrateC. glucoseD. ATPE. lactate

26.5. 0,1,0,1,1NADH is:A. the main factor of catecholamines productionB. inhibitor of Fe2+ oxidation in erythrocytesC. its hydrogen is used in the gluconeogenesisD. necessary for synthesis and secretion of HCl in the stomachE. donor of H+ for Respiratory chain

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27.5. 1,0,1,0,1Which component is common for production of glucose fromalanine and lactate?A. pyruvateB. lactate dehydrogenaseC. Mg2+-ionsD. alanine aminotransferase (glutamic oxaloacetic transaminase,

GOT)E. pyruvate kinase

28.5. 1,0,0,1,1Confirmations are correct:A. monosaccharide has aldehyde-form or keto-formB. monosaccharide has disulfer chemical bondC. monosaccharide includes the peptide chemical bondD. certain carbohydrates have N, P or S-atoms in their structureE. lactose is disaccharide

29.5. 1,1,0,0,0The following statements are correct:A. during reduction monosaccharide is converted into an alcoholB. NAD-dependent enzyme is needed for the reduction of mono-

saccharideC. glucose doesn’t have a reducing propertyD. D-glucose is converted into D-fructose during reductionE. glycosidic bond may be formed with each C-atom

30.5. 1,0,0,1,0The correct statements according to sucrose:A. it is a disaccharideB. it is a heteropolysaccharideC. ribose is a monosaccharide of sucroseD. it is an oligosaccharideE. it is transport form of carbohydrates in plants

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31.5. 1,1,0,0,0Which statements about ribose are correct?A. it can’t be in pyranose-formB. it is a component of certain nucleotidesC. it is a keto-formD. its cyclic form has 5 asymmetric C-atomsE. it has SH-group

32.5. 0,1,1,1,0Which confirmations about lactose and monose are correct?A. they have a b-glycosidic bondB. they have reducing propertiesC. they have the 1,4-glycosidic bondD. they include hexo-aldoses as pyranose-formE. they don’t have reducing properties

33.5. 0,1,0,1,1Digestive mechanism of carbohydrates:A. stomach is the site of carbohydrates hydrolysisB. a-amylase hydrolyzes the a-1,4-glycosidic bonds of homopoly-

saccharidesC. disaccharidases don’t have substrate specificityD. disaccharidases have substrate specificityE. disaccharidases are synthetized into enterocytes

34.5. 0,1,1,1,0Synthesis of glycogen:A. glycogen synthetase “a” forms the a-1,6-glycosidic bondB. glycogen synthetase produces the a-1,4-bond in glycogenC. reaction of glucose activation with UTP is a key oneD. glycogen synthetase “a” is active form after dephosphorylationE. insulin decreases the content of glycogen in the liver

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35.5. 1,1,1,1,0Reaction glucoseà glucose-6-phosphate:A. is irreversible in the cellB. (ATP + Mg2+) complex is needed for this reactionC. product of this reaction is its allosteric inhibitor in the skeletal

musclesD. hexokinase is the enzyme of this reactionE. GTP is a substrate for glucose phosphorylation

36.5. 0,1,0,0,1Phosphofructokinase regulation:A. only ATP and fatty acids are inhibitors of this reactionB. AMP and fructose-1,6-diphosphate are positive modulatorsC. NADPH is the main activator of this reactionD. FMN is the main activator of this reactionE. it is an allosteric enzyme

37.5. 0,1,1,1,0Glycerol phosphate dehydrogenase:A. OH-radical of serine presents in its active centerB. I-CH2-COOH is its inhibitorC. SH-group of cysteine presents in its active centerD. it is enzyme of oxidoreductionE. ATP is a substrate for phosphorylation

38.5. 1,1,0,1,0Production of pyruvate in glycolysis:A. pyruvate kinase is the enzyme of this reactionB. phosphorylation takes place on the substrate levelC. dehydrogenase is the enzyme of this reactionD. 1 ATP molecule is the product of this reactionE. it is a reversible reaction

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39.5. 1,1,1,1,0Substances of glycolysis are:A. lactateB. 2 ATPC. 4 ATPD. 2 NADE. 2 H2O

40.5. 1,0,0,0,1Common enzyme of glycolysis and alcohol oxidation is:A. pyruvate kinaseB. alcohol dehydrogenaseC. lactate dehydrogenaseD. pyruvate decarboxylaseE. hexokinase

41.5. 0,0,0,1,1Common product of glycolysis and alcohol oxidation is:A. acetaldehydeB. lactateC. FADH2D. TPP (TDP)E. pyruvate

42.5. 0,0,1,1,1Pentose phosphate pathway:A. presents only in erythrocytes and hepatocytesB. presents only in the fat tissue and medulla glandsC. is an anabolic pathwayD. produces NADPH and ribose-5-phosphateE. presents in the mitochondria

43.5. 0,0,0,1,1The end product of pentose phosphate pathway is:A. ribulose-5-phosphateB. glucose-6-phosphate

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C. ATPD. ribose-5-phosphateE. 2 NADPH2

44.5. 0,1,1,1,0The end products (before H2O and CO2) of 2 pyruvate molecu-les oxidation are:A. 2 NADHB. 8 NADHC. 2 FADH2D. 30 ATPE. 38 ATP

45.5. 1,0,0,1,1Enzyme of galactose (Gal) metabolism is:A. galactokinaseB. aldolaseC. phosphotaseD. UDP-Gal-pyrophosphorylaseE. UDP-Gal-epimerase

46.5. 0,0,1,1,1Activator of gluconeogenesis is:A. AMPB. insulinC. corticosteroneD. citrateE. ATP

47.5. 0,1,1,1,1Common enzyme of glycolysis and gluconeogenesis is:A. hexokinaseB. enolase (enoylhydratase)C. phosphoglycerate mutase

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D. triose-phosphate isomeraseE. phosphoglycerate kinase

48.5. 1,0,0,1,1Insulin is:A. activator of glucose transport to tissuesB. activator of glycerol convertion into glucoseC. activator of lypolysisD. activator of lipids synthesis in the liverE. activator of glycolysis

LIPIDS: CHEMICAL STRUCTURE AND METABOLISM

1.5. 1,0,0,0,1The main function of lipids is:A. transportB. catalyticC. contractionD. geneticE. energetic

2.5. 0,1,1,0,0Lipids as the components of the cell membrane are:A. trigliceridesB. cholesterolC. phosphodiglycerideD. phosphatidyl ethanolE. free fat acids

3.5. 0,0,0,1,0Neutral lipids are esters of the following components:A. ethanolamine and amino acidsB. sphingosine and fat acidsC. ethylenglycol and fat acidsD. glycerol and fat acidsE. cholesterol and fat acids

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4.5. 0,0,0,1,0The biological role of phosphatidyl choline and phosphatidylethanolamine is:A. the main components of the fat tissueB. substrates of cholesterol productionC. energetic roleD. the main components of the cell membraneE. the main components of the nerve cell membranes

5.5. 0,0,1,0,0Component of phospholipids is the following amino acid:A. methionineB. cysteineC. serineD. tyrosineE. a-alanine

6.5. 0,0,0,0,1What is a ceramide?A. triacylglycerolB. phospholipidsC. plasmalogenD. steridE. sphingomyelin

7.5. 1,0,1,0,0Galactose is the component of:A. cerebrosidesB. gangliosidesC. sulpholipidsD. acetalphosphatidesE. sterids

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8.5. 0,0,1,0,0Sites and enzymes of triglycerides hydrolysis (digestion) are:A. intestinal lipase, the small intestineB. gastric lipase, stomachC. pancreatic and intestinal lipases, the small intestineD. lipoproteinlipase, intestineE. phospholipase, the large intestine

9.5. 0,0,1,1,0The bile acids are products of conjugation with the followingcomponent:A. cholesterolB. serineC. taurineD. glycineE. bilirubin

10.5. 0,0,1,0,0Glycerophospholipids are hydrolyzed by:A. pancreatic lipaseB. intestinal lipaseC. phospholipaseD. coupled (conjugates) bile acidsE. cholesterol esterase

11.5. 0,0,1,0,0Production of lysophosphatidyl choline and lysophosphatidylethanolamine is catalyzed by:A. lipase (intestinal, pancreatic)B. phospholipase A1C. phosphjlipase A2D. phospholipase CE. phospholipase D

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12.5. 0,0,0,1,0Phospholipids may be modified into phosphatidyc acid by actionof:A. phospholipase A1B. phospholipase A2C. phospholipase CD. phospholipase DE. all these enzymes

13.5. 0,0,0,1,0The common intermediate of the triglycerides and phospholi-pids synthesis is:A. diacylglycerolB. triacylglycerolC. phosphoglycerinic acidD. phosphatidyc acidE. monoacylglycerol

14.5. 0,0,0,1,0Chylomicrons are broken down by the action of:A. triglyceridlipaseB. diglyceridlipaseC. monoglyceridlipaseD. lipoproteinlipaseE. phospholipase

15.5. 0,1,0,0,0The hormone-sensitive enzyme and hormones of fat acids mo-bilization are:A. digliceridlipase insulinB. triglyceridlipase glucagon, catecholaminesC. monoglyceridlipase catecholaminesD. triglyceridlipase steroid hormonesE. diglyceridlipase catecholamines, glucagon

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16.5. 0,0,1,0,0Triglyceridlipase is activated by adrenalin and glucagon viathe second messenger:A. inosytol mechanismB. cTMPC. cAMPD. Ca2+-ionsE. production of enzymes by genome activation

17.5. 0,0,1,0,0The common intermediate of the carbohydrates and glycerolcatabolism is:A. glyceraldehyde-3-phosphateB. 3-phosphoglycerinic acidC. dihydroxyacetone phosphateD. 2-phosphoglycerinic acidE. 1,3-diphosphoglycerinic acid

18.5. 0,0,0,1,0Transport of fatty acids from cytosol into mitochondria takesplace in the form of:A. free fat acidB. acyl-coAC. acyl-coQD. acylcarnetineE. acyl-coA and acylcarnetine

19.5. 0,1,0,0,0Number of acetyl-coA and cycles which are as the result of b-oxidation of the fat acid with 14 carbon atoms:A. 7 and 7B. 7 and 6C. 6 and 7D. 6 and 6E. 7 and 5

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20.5. 0,0,0,1,0The ketone bodies are:A. acetone, b-ketobutiric acid, valerianic acidB. acetoacetic acid, a-hydroxybutiric acid, acetonC. b-hydroxybutiric acid, a-ketobutiric acid, acetonD. acetoacetic acid, b-hydroxybutiric acid, acetonE. acetic acid, butiric acid, aceton

21.5. 0,0,0,1,0Aceton is produced during the following process:A. b-oxidation of fatty acidsB. glycolysisC. glycerol catabolismD. decarboxylation of acetoacetic acidE. reduction of glyceraldehyde-3-phosphate

22.5. 0,1,0,0,0Which substance is the donor of methyl-group for phosphati-dylcholine production?A. methionineB. S-adenosylmethionineC. S-adenosylhomocysteineD. methilcobalamineE. tetrahydrofolic acid

23.5. 0,0,1,0,0Which type of acid-base disorders does take place in the bloodin patients with diabetes mellitus?A. metabolic alkalosisB. gaseous (respiratory) acidosisC. metabolic acidosisD. gaseous (respiratory) alkalosisE. mixed acidosis

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24.5. 0,0,0,1,0For phosphatidylcholine production is needed:A. ADPB. TTPC. GTPD. CTPE. UTP

25.5. 0,0,1,0,0For synthesis of conjugated bile acids are needed:A. taurine and cholesterolB. cysteine and uronic acidsC. glycocoll and cholic acidD. methionine and deoxycholic acidE. taurine and chenodeoxycholic acid

26.5. 0,1,0,1,0Phospholipids of the membranes:A. soluble in waterB. are polar moleculesC. are nonpolar moleculesD. have electric chargeE. don’t have electric charge

27.5. 1,1,1,0,0Functions of the cell membranes are:A. receptoricB. permeabilityC. compartmentalizationD. glycolytical enzymes present in the cell membraneE. prodaction of oxyhemoglobine (HbO2)

28.5. 0,1,1,0,0Principal protein of the cell membranes is:A. albuminB. glycophorin

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C. spectrinD. collagenE. calmodulin

29.5. 0,1,0,0,0Glycerol is:A. dihydroxyalcoholB. trihydroxyalcoholC. cyclic alcoholD. aldehydeE. ketone

30.5. 0,0,1,1,0Unsaturated fatty acid is:A. palmiticB. lauricC. linolenicD. arachidonicE. stearic

31.5. 1,0,0,1,1Saturated fatty acid is:A. capronicB. oleicC. linolenicD. stearicE. palmitic

32.5. 0,1,0,1,1The structural component (alcohol) of phospholipids is:A. cholesterolB. inositolC. hydroxychinolD. glycerolE. glycerolphosphate

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33.5. 0,0,1,0,0Which lipid is ceramide?A. triacylglycerolB. phosphatidylcholineC. sphingomielinD. gangliosideE. plasmalogen

34.5. 0,0,1,0,0Sphingosin presents in the following lipids:A. glycerophospholipidsB. lysophosphatidylcholinesC. glycolipidsD. a-lipoproteinsE. b-lipoproteins

35.5. 0,0,1,0,0Oligosaccharide of galactose presents in the following lipids:A. sulpholipidsB. cerebrosidesC. gangliosidesD. sphingomielinsE. plasmalogenes

36.5. 0,1,0,1,1Cholesterol is substrate for synthesis of:A. vitamin KB. vitamin DC. vitamin ED. bile acidsE. testosteron

37.5. 0,1,1,0,1Bile acids are:A. lignoceric

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B. cholicC. glycocholicD. phosphocholicE. deoxycholic

38.5. 0,0,0,0,1The main functions of triacylglycerins:A. permeability of the cell membraneB. transport of substances via membraneC. transfer of the nerve impulseD. intercellular interrelationsE. energetic storage

39.5. 0,0,0,1,0Lysophosphatidylcholin is product of phospholipid hydrolysis by:A. phospholipase CB. phospholipase DC. pancreatic lipaseD. phospholipase A2E. intestinal lipase

40.5. 0,0,1,0,0The main components of chylomicrons are:A. proteinsB. phospholipidsC. triglyceridesD. cholesterolE. cholesterides

41.5. 0,1,0,0,0The enzyme for mobilization of the neutral lipids is:A. diglyceride lipaseB. triglyceride lipaseC. monoglyceride lipaseD. all these enzymesE. intracellular phospholipase

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42.5. 0,0,1,0,0The secondary messenger of adrenalin action for lipids mobili-zation is:A. inositolB. 3’,5’-cCMPC. 3’,5’-cAMPD. Ca2+-ionsE. oligonucleotide

43.5. 0,0,1,0,0The product of first reaction of glycerol oxidation is:A. glyceraldehyde-3-phosphateB. dihydroxyacetone phosphateC. glycerol-3-phosphateD. phosphoglycerinic acidE. diglycerophosphate

44.5. 0,0,1,0,0The product of glycerolphosphate oxidation is:A. phosphoglycerinic acidB. 3-glycerinic acidC. dihydroxyacetone phosphateD. phosphoenolpyruvateE. glyceraldehyde-3-phosphate

45.5. 1,0,1,1,0The mechanism activation of fatty acids is needed of:A. carnetine + ATPB. ATP + coQC. HS-coA + ATPD. biotin + ATPE. carnosine + ATP

46.5. 0,1,1,0,0Enzyme of fatty acids activation is:A. carnetine-acyl-ScoA synthetase

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B. tiokinaseC. acyl-ScoA synthetaseD. acyl-ScoQ synthetaseE. acyl-ScoA transferase

47.5. 0,0,0,1,0The transport form of fatty acid in mitochondria is:A. free fatty acidB. acyl-ScoAC. acyl-ScoQD. acyl-carnetineE. acyl-ScoA and carnetine

48.5. 0,0,1,0,0The products of the first reaction of b-oxidation of fatty acid are:A. acyl-ScoA + FADH2B. enoyl-ScoA + NADHC. trans-enoyl-ScoA + FADH2D. cetoacyl-ScoA + FMNE. hydroxyacyl-ScoA + FADH2

49.5. 0,0,0,01What are the products of thiolyzation of fatty acid?A. acyl-ScoA + HS-coAB. acyl-scoAC. acetoacetyl-ScoA + HS-coAD. acyl + acetyl-ScoAE. acyl-ScoA + acetyl-ScoA

50.5. 0,0,1,0,0Number of acetyl-ScoA for synthesis of acetoacetic acid is:A. 1B. 2C. 3D. 4E. 6

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51.5. 0,0,0,1,0Aceton is produced in:A. b-oxidation of fatty acidsB. glycolysisC. glycerol metabolismD. acetoacetic acid decarboxylationE. in glycerol-3-phosphate oxidation

52.5. 0,0,1,0,0The major portion of fatty acids synthetizes in:A. nucleusB. mitochondriaC. cytoplasmD. chromosomeE. endoplasmic reticulum

53.5. 0,0,1,0,0Acetyl-ScoA moves from mitochondria to cytoplasm as:A. acyl-carnetineB. its free formC. citrateD. acetoacetyl-ScoAE. acetoacetate

54.5. 0,0,0,1,0Which components are needed for breakdown of citrate in cy-tosol?A. ATP + kinaseB. GTP + kinaseC. HS-coA + thiolaseD. ATP + HS-coA + ATP-citrate lyaseE. ATP + citrate lyase

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55.5. 0,0,0,1,0The activator and inhibitor of acetyl-ScoA carboxylase are:A. malonate ADPB. succinate citrateC. acetoacetate NADHD. citrate palmitoyl-ScoAE. ATP FADH2

56.5. 0,0,0,1,0The reaction for transformation of acetoacetyl-ScoA in fattysynthesis is:A. dehydrogenationB. decarboxylationC. hydrolysisD. hydrotationE. dehydrotation

57.5. 0,0,1,0,0Hydrogen (H+) donor of acetoacetyl-ScoA reduction is:A. NADHB. FADH2C. NADPH2D. FMNH2E. TDP

58.5. 0,0,0,1,0The product of the first cycle of fatty synthesis and number ofNADPH are:A. crotonyl-SACP 2 NADPHB. acetoacetyl-SACP 3 NADPHC. b-hydroxibutiryl-SACP 2 NADPHD. butiryl-SACP 2 NADPHE. butiryl-SACP 4 NADPH

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59.5. 0,0,1,1,0The site for elongation of fatty acid chain is:A. hialoplasmB. mitochondriaC. endoplasmic reticulum (EPR)D. mitochondria and endoplasmic reticulumE. microsomes

60.5. 1,0,0,0,0The enzyme of production of mono- and polyenic fatty acids is:A. monooxygenaseB. dehydrogenaseC. dioxygenaseD. hydrotaseE. dehydrotase

61.5. 1,1,1,1,1Isopren-group presents in the chemical structure of the follo-wing biological active substances:A. vitamin AB. vitamin EC. vitamin KD. cholesterolE. side-radical of chlorophyls

62.5. 0,0,1,0,0The common intermediate of TAG and phospholipids byosyn-thesis is:A. monoglycerideB. diglycerideC. diacylglycerol-3-phosphateD. glycerol-3-phosphateE. monoacylglycerol phosphate

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63.5. 0,0,1,0,0Which substance is specific for the lipids synthesis?A. ADPB. TTPC. CTPD. GTPE. UTP

64.5. 0,0,1,0,0The initial reaction of the phospholipids synthesis is:A. phosphatidic acid + ATPB. phosphatidic acid + GTPC. phosphatidic acid + CTPD. phosphatidic acid + TTPE. phosphatidic acid + UTP

65.5. 0,0,0,1,0Convertion of phosphatidyl ethanolamine into phosphatidylcholine requires:A. 2 CH3-groupsB. 1 CH3-groupC. 4 CH3-groupsD. 3 CH3-groupsE. carboxylation

66.5. 0,1,0,0,0The role of adrenalin and glucagon in the lipid metabolism re-gulation is:A. activation of adenylate cyclase productionB. activation of adenylate cyclase activityC. activation of phosphodiesteraseD. inhibition of adenylate cyclaseE. inhibition of triglyceride lipase

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67.5. 0,1,0,0,0In the lipid metabolism regulation insulin is:A. activator of adenylate cyclaseB. activator of phosphodiesterase synthesisC. activator of phosphodiesteraseD. inhibitor of adenylate cyclaseE. activator of triglyceride lipase

68.5. 0,0,1,0,0The metabolic disturbance in patients with diabetes mellitus is:A. metabolic alkalosisB. respiratory acidosisC. metabolic acidosisD. gaseous alkalosisE. metabolic and gaseous acidosis

69.5. 0,0,0,1,0Hyposecretion of bile in patient dues to hypovitaminoses:A. A, B6, B12B. E, B12, PPC. D, B1, B6D. K, EE. B5, H, PP

70.5. 0,1,0,0,0Lipotropic substances are:A. vitamins B1, B2, B6B. methionine, S-adenosylmethionineC. cystein, S-adenosylhomocysteinD. adrenalin, noradrenalinE. insulin, glucagon

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71.5. 0,0,0,0,1Which atoms of glucose aren’t used for fatty acids synthesis?A. 1 and 5B. 2 and 4C. 3 and 6D. 1 and 4E. 3 and 4

72.5. 0,0,1,1,1Bile acid is:A. arachidonic acidB. glyco-arachidonic acidC. choleic acidD. glycocholic acidE. taurocholic acid

CATABOLISM OF SIMPLE PROTEINS.METABOLISM OF NUCLEOPROTEINS AND

CHROMOPROTEINS

1.5. 0,1,1,1,0Biological functions of proteins are:A. coenzymicB. catalyticalC. plasticD. transportE. energetic

2.5. 0,1,0,1,0The essential amino acids are:A. arginineB. tryptophanC. glutamic acidD. phenylalanineE. tyrosine

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3.5. 0,1,1,0,1HCl functions are:A. activation of trypsinogenB. activation of pepsinogenC. optimum pH for pepsin activityD. optimum pH for lipase activityE. denaturation of food proteins

4.5. 1,0,1,0,1Characteristics of pepsin are:A. it secretes from the main mucosal cells of the stomachB. it secretes from additional mucosal cells of the stomachC. it is activated by HCl in the stomach cavityD. its optimum pH is 3,0-4,0E. its optimum pH is 1,5-2,5

5.5. 1,0,1,0,1Characteristics of trypsin are:A. it secretes in the nonactive form as trypsinogenA. it is an exopeptidaseB. enterokinase is an activator of trypsinogenC. intestine is the site of trypsinogen secretionD. mechanism of the trypsinogen activation is a partial proteolysis

6.5. 0,1,0,1,0Characteristics of trypsin and enterokinase are:A. trypsin hydrolyzes the peptide bonds between lys and arg at

N-positionB. trypsin hydrolyzes the peptide bonds between lys and arg at

C-positionC. optimum pH of trypsin is 7,2-7,8D. optimum pH of trypsin is 8,2-8,8E. active enterokinase is glycoprotein

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7.5. 0,1,0,1,0Chymotrypsin:A. secretes of the intestinal mucosal cellsB. secretes of the pancreatic glandC. is an exopeptidaseD. is an endopeptidaseE. is an activator of trypsinogen

8.5. 0,0,1,0,1Carboxypeptidases:A. secret in active formsB. are the endopeptidasesC. carboxypeptidase A is a Zn-containing enzymeD. are nucleoproteinsE. are metaloproteins

9.5. 0,1,1,0,0Aminopeptidases:A. are endopeptidasesB. are exopeptidasesC. break a N-end amino acidsD. have an absolute specific activityE. Mg2+ is аn activator of aminopeptidase

10.5. 0,1,1,0,0Dipeptidases:A. are endopeptidasesB. are exopeptidasesC. hydrolyze the dipeptidesD. are elastasesE. secret of the mucosal cells of the stomach

11.5. 0,1,0,1,0Absorption of amino acids:A. is a simple diffusion

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B. is an active diffusionC. uses the Ca+-ATP-aseD. uses the Na+,K+-ATP-aseE. is antiport of Na+-ions diffusion

12.5. 0,1,1,0,0Absorption of amino acids:A. takes place in the stomachB. takes place in the small intestineC. is needed the Na+-ionsD. is needed the Ca2+-ionsE. takes place in the large intestine

13.5. 1,0,0,1,0g-Glutamyl transferase:A. has the cofactor - glutathioneB. has the cofactor - cysteineC. has the cofactor – glutamic acidD. uses the energy of glutathione bondsE. uses the energy of ATP

14.5. 1,0,1,0,0Putrefaction of amino acids in the intestine produces:A. toxic substances in large intestineB. toxic substances in small intestineC. indoleD. histamineE. hippuric acid

15.5. 1,0,0,1,1Putrefaction of amino acids in intestine produces:A. cadaverineB. indikanC. indole as a toxic product of tyrosine degradationD. indole as a toxic product of tryptophan degradationE. phenol as a product of tyrosine degradation

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16.5. 0,1,0,0,1Amino acids are used for production of:A. uric acidB. ureaC. ATPD. ketone bodiesE. creatinine

17.5. 0,1,0,1,0The main pathways of amino acids catabolism are:A. isomerizationB. transaminationC. epimerizationD. deaminationE. transmethylation

18.5. 1,0,0,1,0Types of amino acids deamination in the human tissues:A. direct oxidative deaminationB. hydrolytical deaminationC. intramolecular deaminationD. indirect oxidative deaminationE. reductive deamination of glutamic acid

19.5. 1,0,0,0,0Direct oxidative deamination is correct for:A. glutamic acidB. aspartic acidC. glycineD. serineE. alanine

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20.5. 0,0,1,0,1Indirect deamination is correct for:A. glutamic acidB. asparagineC. aspartic acidD. serotoninE. alanine

21.5. 0,1,0,1,1Transamination is correct for:A. tryptamineB. glutamic acidC. serotoninD. aspartic acidE. alanine

22.5. 1,0,0,1,0Reaction: HOOC-CH2-CHNH2-COOH + HOOC-(CH2)-CO-COOH àHOOC-CH2 –CO-COOH + HOOC-(CH2)2-CHNH2-COOHA. is transaminationB. is decarboxylationC. is the direct oxidative deaminationD. is the reaction of AsAT (GOT)E. is the reaction of AlAT (GPT)

23.5. 0,1,1,0,0Transamination of alanine is:A. the production of oxaloacetateB. the production of pyruvateC. the reaction catalyzed by AlAT (GPT)D. an indirect processE. synthesis of biogenic amine

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24.5. 0,1,1,0,0Decarboxylation of amino acids:A. is production of ketone bodiesB. is production of biogenic aminesC. vitamin B6 is necessary as coenzymeD. vitamin B1is necessary as coenzymeE. produces ammonia (NH3)

25.5. 1,0,1,0,0Decarboxylation of histidine:A. is production of histamineB. is production of GABAC. pyridoxal phosphate is necessary as coenzymeD. NAD is necessary as coenzymeE. is production of serotonin

26.5. 0,1,1,0,0Decarboxylation of hydroxytryptophan:A. is production of histamineB. is production of serotoninC. is synthesis of hydroxytryptamineD. NAD is necessary as coenzymeE. is catalyzed by AlAT (GPT)

27.5. 1,0,0,1,0Amino acids as precursors (substrates) of catecholamines pro-duction are:A. phenylalanineB. glutamic acidC. arginineD. tyrosineE. glycine

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28.5. 1,0,0,1,0Production of ammonia (NH3) in the cells:A. direct oxidative deaminationB. transamination of amino acidsC. decarboxylation of histidineD. indirect oxidative deamination of alanineE. reductive amination of glutamic acid

29.5. 1,0,1,0,0Urea production:A. takes place in the hepatocytesB. takes place in the kidneysC. is ornithine cycleD. is needed for vitamin B1E. is needed for arginine

30.5. 1,0,1,0,0Final products of ammonia detoxication are:A. ureaB. uric acidC. ammonia saltsD. carbamoylphosphateE. glutamine

31.5. 1,0,0,1,0Methionine is:A. an essential amino acidB. a nonessential amino acidC. a basic amino acidD. a donor of CH3 groupE. a donor of disulphide (S-S) bonds in the proteins structure

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32.5. 0,1,1,0,0For purine nucleotide production is necessary:A. carbomoylphosphateB. glycineC. inosine acidD. adenosine phosphateE. vitamin B1

33.5. 1,0,0,1,1For pyrimidine nucleotide production is necessary:A. carbomoyl-phosphateB. inosine acidC. vitamine B6 as coenzymeD. aspartic acidE. glutamine as a donor of amino group for CMP

34.5. 0,1,1,0,0Monoaminooxidase is enzyme:A. for the biogenic amines productionB. for the biogenic amines inactivationC. of histamine inactivationD. catalyzes the production of serotoninE. as the TDP-dependent one

35.5. 1,0,1,0,0Allopurinol:A. is the inhibitor of the uric acid productionB. is the activator of the uric acid productionC. decreases the uric acid concentration in the bloodD. increases the uric acid concentration in the bloodE. is the substrate of xantine oxidase

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36.5. 0,1,0,1,0HOOC-CH2-CH2-CH-COOH | NH2This substance is:A. aspartic acidB. glutamic acidC. essential amino acidD. nonessential amino acidE. asparagine

37.5. 0,1,0,1,0Hyppuric acid is:A. complex of acetyl-ScoA and glycineB. complex of benzoic acid and glycineC. conjugate of phenol and glycineD. conjugate of benzoic acid and glycineE. complex of indol and glycine

38.5. 0,1,0,1,1HOOC-CH-CH2-CH2-COOHàEàH2N-CH2-CH2-CH2COOH+ CO2 | NH2This reaction:A. is carboxylationB. is decarboxylationC. vitamin B2 is necessary for itD. vitamin B6 is necessary for itE. is production of GABA

39.5. 1,0,1,1,0 R-CH2-NH2 + H2Oà Eà R-COH + NH3 + H2O2This reaction:A. is inactivation of the biogenic amines

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B. is production of the hormonoidesC. is inactivation of histamineD. is oxidative deamination of aminesE. is hydrolysis of the biogenic amines

40.5. 0,1,0,0,1Amino acids as precursors of the catecholamines productionare:A. glutamic acidB. phenylalanineC. histidinD. aspartic acidE. tyrosine

41.5. 0,1,0,0,0Amino acid as precursor of histamine synthesis is:A. glutamic acidB. histidinC. glutamineD. aspartic acidE. methionine

42.5. 0,0,1,1,0Amino acid needed for serotonin synthesis is:A. phenylalanineB. tyrosineC. tryptophanD. hydroxytryptophanE. tryptamine

43.5. 1,0,1,1,0Final products of the simple proteins catabolism are:A. ammoniaB. glutamine

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C. ureaD. CO2E. uric acid

44.5. 0,1,1,0,0HOOC-CH-CH2-CH2-COOH + NH3àEà HOOC-CH-CH2-CH2-CONH2 | | NH2 NH2This reaction:A. is amination of aspartic acidB. catalyzes by glutamine synthetaseC. is production of glutamineD. is production of asparagineE. catalyzes by asparagine synthetase

45.5. 1,0,1,1,0 Choose the correct reactions of urea production:A. carbamoylphosphate + ornithineà citrulline + H3PO4B. carbamoylphosphate + ornithine + ATPà citrulline + ADP +

H3PO4C. citrulline + aspartate + ATPà argininosuccinate + AMP + PPD. argininosuccinateà arginine + fumarateE. argininosuccinate + H2Oà arginine + fumarate

46.5. 1,1,0,1,0Amino acids and derivatives which are used in urea produc-tion are:A. glutamineB. aspartic acidC. threonineD. arginineE. glutamic acid

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47.5. 0,0,1,0,0The number of ATP which produced during a full degradationof alanine is:A. 4B. 18C. 15D. 22E. 12

48.5. 0,1,0,1,0Substances for ammonia salts synthesis are:A. glutamic acidB. glutamineC. ureaD. CO2E. aspartic acid

49.5. 0,0,1,0,1Amino acids which may be synthetized from intermediates ofthe Krebs cycle are:A. alanineB. serineC. aspartic acidD. tyrosineE. glutamic acid

50.5. 0,0,0,1,0The site of the direct deamination of amino acid is:A. nucleusB. cytoplasmC. ribosomeD. mitochondriaE. lyzosome

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51.5. 0,1,0,1,1Sources of NH3 in the human organism are:A. a-ketoglutarateB. adenineC. pyruvateD. glutamineE. asparagine

52.5. 0,1,1,1,0For detoxication and transport of NH3 are needed:A. citrullineB. glutamateC. glutamineD. aspartic acidE. ornithine

53.5. 1,0,0,1,0Glutamate dehydrogenase is:A. oxido-reductaseB. hydrolaseC. isomeraseD. hydrogenaseE. transferase

54.5. 0,0,1,0,1End products of ammonia detoxication are:A. glutamineB. asparaginesC. ureaD. uric acidE. ammonia salts

55.5. 0,0,1,0,1Transport form of ammonia in the blood is:A. carbamoylphosphate

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B. uric acidC. glutamineD. glutamic acidE. asparagine

56.5. 0,1,1,0,1Interrelations between the Krebs cycle and urea productioncycle:A. NADH2 produced in the Krebs cycle is used in the urea pro-

ductionB. CO2 produced in the Krebs cycle is used into in the urea cycleC. fumarate produced in the urea cycle is used in the Krebs cycleD. fumarate produced in the Krebs cycle is used in the urea cycleE. the Krebs cycle generates the ATP for the urea cycle

57.5. 0,1,0,1,1Glycine is needed for synthesis:A. pyrimidine nucleotidesB. hemeC. indicanD. hippuric acidE. glutathione

58.5. 1,1,0,1,1Glutathione:A. is a tripeptideB. is a coenzymeC. has only reduced formD. is an antioxidantE. includes glutamic acid

59.5. 1,0,1,1,0Characteristics of glutathione reductase (GR) and glutathioneperoxidase (GP):A. glutathione is a substrate for GR

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B. glutathione is a coenzyme for GRC. glutathione is a substrate for GPD. GP uses of the reduced form of glutathione (GSH)E. GR uses of the reduced form of glutathione (GSH)

60.5. 0,1,1,0,1Cysteine:A. is a nonessential amino acidB. is an essential amino acidC. is a thioamino acidD. is a hydroxyamino acidE. presents in the active centers of enzymes

61.5. 1,0,0,1,1Phenylalanine:A. is an essential amino acidB. is a nonessential amino acidC. in the human organism it may be synthetized from fenolic acid

and alanineD. is used in the synthesis of catecholaminesE. is used in the synthesis of thyroxine

62.5. 0,1,0,0,1Tryptophan is:A. a nonessential amino acidB. an essential amino acidC. used in the synthesis of catecholaminesD. used in the synthesis of adrenalinE. used in the synthesis of serotonin

63.5. 1,0,1,0,1Histidine:A. is an essential amino acidB. is a nonessential amino acidC. is used in the histamine production

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D. is used in the GABA productionE. vitamin B6 is necessary for its decarboxylation

64.5. 1,1,0,1,1Glutamic amino acid is:A. a nonessential amino acidB. an acidic amino acidC. an intermediate of urea productionD. an acceptor of NH3E. a substrate for purine nucleotides synthesis

65.5. 1,0,1,1,1Glutamic acid is used for synthesis of:A. glutamineB. asparagineC. purine nucleotidesD. glutathioneE. carbamoylphosphate

66.5. 0,1,1,0,0Characteristics of digestive mechanism of nucleoproteins (NP)in the gastro-intestinal tract are:A. breakdown of nucleic acids takes place in the stomachB. stomach is the site of NP hydrolysisC. hydrolases are necessary for breakdown of NPD. only trypsin is an enzyme for breakdown of NPE. only pepsin is needed for breakdown of NP

67.5. 0,0,1,1,1Final products of purine nucleotides degradation are:A. xantinB. b-alanineC. CO2D. uric acidE. H2O

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68.5. 1,0,0,1,1Final products of pyrimidine nucleotides degradation are:A. ureaB. uric acidC. xantinD. b-alanineE. CO2

69.5. 1,1,0,1,0For heme synthesis the following compounds are necessary:A. glycineB. succinyl-ScoAC. aspartateD. key enzymes, d-aminolevulinate synthetase and ferrohelataseE. only a key enzyme, d-aminolevulinate synthetase

70.5. 1,0,0,1,1Name the substances needed for heme synthesis:A. vitamin B12B. vitamins B1 and HC. vitamin H and S-adenosyl-methionineD. pyridoxal phosphateE. d-aminolevulinate synthetase as an allosteric enzyme

71.5. 0,1,1,0,1Hemoglobin degradation:A. takes place in all human organsB. sites for breakdown of Hb are liver, spleen, marrow cellsC. NADP-oxidase is an enzyme for verdoglobin productionD. NAD-oxidase is enzyme of verdoglobin productionE. verdoglobin breaks down to Fe, globin and biliverdin

72.5. 0,0,1,1,1Bilirubin conjugation, name the correct characteristics:A. its enzyme is bilirubin reductase

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B. site for this process is mitochondriaC. its enzyme is bilirubin glucoronyltransferaseD. its enzyme is bilirubin UDP-GA-transferaseE. indirect bilirubin + UDP-GAà direct bilirubin + UDP

73.5. 0,1,1,0,1Direct bilirubin:A. is hydrophylic substanceB. is hydrophobic substanceC. is nontoxic substanceD. is toxic substanceE. penetrates the cell membranes

74.5. 1,0,0,1,1Indirect bilirubin:A. penetrates the cell membranesB. doesn’t penetrate the cell membranesC. is nontoxic substanceD. is toxic substanceE. combines with albumine in the blood

HORMONES: CHEMICAL STRUCTURE, MECHANISMACTION, METABOLIC ROLE

1.5. 1,0,1,0,1Hormones are:A. simple proteinsB. carbohydratesC. complex proteinsD. glucose derivativesE. steroids

2.5. 0,1,0,1,1Mechanism of hormonal action:A. g-peptidase

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B. membrane (membranous)C. localD. membrane intracellular or indirectE. cytosolic or direct

3.5. 1,0,0,1,0Hormone mechanism of action is:A. centralB. NAD-dependentC. localD. peripheralE. TDP-dependent

4.5. 0,1,0,0,0Membrane mechanism is:A. specific for glucagonB. specific for insulinC. 2,3-cAMP-dependentD. characteristic for steroid hormonesE. characteristic for thyroxine

5.5. 1,0,0,1,0Name the correct statements of adenylate cyclase:A. 3,5-cAMP is its productB. 2,3-cAMP is its productC. 3,5-cGMP is its productD. ATP is its substrateE. ADP is its substrate

6.5. 0,0,1,1,03,5-cAMP is a:A. substrate of guanylate cyclaseB. cyclic dinucleotideC. cyclic mononucleotideD. secondary messengerE. primary mediator

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7.5. 0,1,0,1,03,5-cGMP is a:A. substrate of adenylate cyclaseB. substrate of guanylate cyclaseC. product of ATPD. product of GTPE. primary mediator

8.5. 1,1,0,1,0Secondary messengers are:A. 3,5-cAMPB. 3,5-cGMPC. 2,3-cAMPD. Ca2+-ionsE. Mg2+-ions

9.5. 1,0,0,1,0Specificity of hormone:A. 3,5-cAMP is secondary messenger of glucagonB. glucagon is activator of gluconeogenesisC. hydrocortisone is activator of gluconeogenesisD. adrenalin is activator of glycogenolysisE. adrenalin is activator of glycogen production

10.5. 0,1,1,0,1Adrenalin:A. is a hypoglycemic hormoneB. is a hyperglycemic hormoneC. 3,5-cAMP is a secondary messenger of adrenalinD. 2,3-cAMP is a secondary messenger of adrenalinE. has a- and b-receptors on the cell membrane

11.5. 1,0,0,1,1Glucagon:A. is a hyperglycemic hormone

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B. is a hypoglycemic hormoneC. 3,5-cGMP is a secondary messenger of glucagonD. is activator of glycogenolysisE. a-cells of the pancreatic gland secrete glucagon

12.5. 1,0,1,0,1Insulin is a:A. simple proteinB. complex proteinC. hormone with the membrane mechanism of actionD. hyperglycemic hormoneE. hypoglycemic hormone

13.5. 1,0,0,1,0Insulin is:A. an anabolic hormoneB. a catabolic hormoneC. amino acid derivativesD. a dimer in active formE. a trimer in active form

14.5. 0,1,1,0,0Hypothalamic hormones are:A. complex proteinsB. polypeptidesC. liberins and statinsD. somatotropinsE. corticotropins

15.5. 1,0,1,0,1Hypophyseal hormones are:A. somatotropinB. somatoliberinC. thyrotropinD. thyroliberinE. lutropin

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16.5. 1,0,0,1,1Vasopressin is an:A. activator of water reabsorbtion in the distal tubes of the kidneysB. diuretic hormone (increases of diures)C. activator of cGMP protein kinasesD. activator of cAMP protein kinasesE. antidiuretic hormone

17.5. 0,1,0,1,1Somatotropin:A. is a catabolic hormoneB. acts via 3,5-cAMP secondary messengerC. acts via 3,5-cGMP secondary messengerD. is a growth hormoneE. is an anabolic hormone

18.5. 1,1,0,0,1Thyroidal hormones:A. are iodothyroninesB. thyroxine is tetraiodothyronineC. thyroxine is a complex proteinD. thyroxine has the membrane mechanism of actionE. calcitonin is a hormone of thyroidal gland

19.5. 1,1,0,1,0Calcitonin and parathyrin:A. are hormones of parathyroid glandsB. calcitonin is a hormone of thyroid and parathyroid glandsC. calcitonin increases Ca2+-ions concentration in the bloodD. calcitonin decreases Ca2+-ions concentration in the bloodE. parathyrin decreases Ca2+-ions concentration in the blood

20.5. 1,0,0,1,0Pancreas hormones:A. insulin is secreted of b-cells of the pancreas

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B. insulin is secreted of a-cells of the pancreasC. glucagon is secreted of b-cells of the pancreasD. insulin is a hypoglycemic hormoneE. glucagon is a hypoglycemic hormone

21.5. 1,1,0,0,1Adrenal cortex hormones:A. are steroid hormonesB. are corticosteroidsC. have the membrane mechanism of actionD. are derivatives of amino acidsE. cholesterol is a substrate for production of aldosterone

22.5. 0,0,1,0,1Aldosterone is a:A. simple proteinB. regulator of Ca2+-ions concentration in the bloodC. mineralocorticoidD. glucocorticoidE. regulator of Na+ and K+ concentration in the blood

23.5. 1,0,1,0,0Glucocorticoids:A. are steroid hormonesB. decrease the glucose concentration in the bloodC. increase the glucose concentration in the bloodD. have the the membrane mechanism of actionE. have the cytosolic (direct) mechanism of action

24.5. 1,0,0,1,1Sex hormones:A. are steroid hormonesB. are catabolic hormonesC. have the membrane-cytosolic mechanism of actionD. estradiol and testosterone are sex hormonesE. have the direct (cytosolic) mechanism of action

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25.5. 0,0,1,1,0Prostaglandins:A. are steroid hormonesB. have the membrane-cytosolic mechanism of action via

3,5-cAMPC. are the hormone-like compounds (hormonoids)D. are compounds derived from C20-polyene fatty acidsE. have an antihormonal action

26.5. 0,1,1,1,0Characteristics of hormones are:A. universal actionB. specific propertyC. tropical actionD. systemic actionE. local action

27.5. 0,1,1,0,0Receptors of hormones are:A. lipoproteinsB. glycoproteinsC. specific for hormonesD. phospholipidsE. nucleoproteins

28.5. 0,1,1,1,1Mechanism of hormonal action:A. localB. membraneC. membrane cytosolicD. cytosolicE. indirect

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29.5. 0,1,1,0,1Hormone classifications are:A. physico-chemicalB. biologicalC. chemicalD. functionalE. based on the mechanism of action

30.5. 0,1,1,1,0 The following hormones have the membrane cytosolic mecha-nism of action:A. thyroxineB. adrenalinC. glucagonD. calcitoninE. insulin

31.5. 0,0,1,1,1The following hormones have the cytosolic mechanism of ac-tion:A. adrenalinB. insulinC. thyroxineD. cortisolE. testosterone

32.5. 0,1,1,1,03’,5 -cAMP:A. is the primary mediatorB. is the secondary mediatorC. is the secondary messengerD. phosphodiesterase decreases 3’,5’-cAMP concentration in the

cellE. phosphodiesterase increases 3’,5’-cAMP concentration in the cell

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33.5. 0,1,1,0,1Protein kinase characteristics are:A. the 3’,5’-cAMP is its inhibitorB. the 3’,5’-cAMP is its activatorC. it is the allosteric enzymeD. dissociation of protein kinase is a irreversible processE. dissociation of protein kinase is a reversible process

34.5. 0,1,1,1,0Hormones are:A. carbohydrates derivativesB. simple proteinsC. complex proteinsD. amino acids derivativesE. sphingosine derivatives

35.5. 0,1,1,1,0Liberins are:A. somatotropinB. prolactoliberinC. thyreoliberinD. corticoliberinE. oxytocin

36.5. 0,1,1,0,1Statins and their characteristics:A. it is cortisolB. it is somatostatinC. it is prolactostatinD. 3’,5’-cGMP is their secondary messengerE. 3’,5’-cAMP is their secondary messenger

37.5. 0,1,1,0,0Hormones of hypophysis and their characteristics:A. they are derivatives of amino acids

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B. they are simple and complex proteinsC. vasopressin deposites in hypophysisD. vasopressin synthetizes in hypophysisE. antidiuretic hormone synthetizes in hypophysis

38.5. 0,1,1,0,0Vasopressin and oxytocin, the correct statements:A. can’t be synthetized in laboratoryB. may be synthetized in laboratoryC. are nonapeptidesD. are octapeptidesE. are decapeptides

39.5. 0,1,1,1,0Vasopressin:A. is an octapeptideB. increases absorption of H2OC. 3’,5’-cAMP is its secondary messengerD. its hyposecretion is due to diabetes insipidusE. its hypersecretion is due to diabetes insipidus?40.5. 1,0,0,0,1Corticotropical hormone (Corticotropin, ACTH):A. is activator of corticosteroids secretionB. is activator only of glucocorticoidsC. is activator only of mineralocorticoidsD. has a steroid natureE. has a proteinic nature

41.5. 1,0,1,0,1Somatotropical hormone (somatotropin, STH) is:A. a simple proteinB. a complex proteinC. synthetized as prohormone

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D. inhibitor of insulin secretionE. inhibitor of lipolysis

42.5. 1,0,0,1,1Thyrotropical hormone (thyrotropin, TTH):A. is a glycoproteinB. is a simple proteinC. 3’,5’-cGMP is its effectorD. 3’,5’-cAMP is its effectorE. has an indirect mechanism of action

43.5. 1,0,1,0,1Parathormone (parathyrin):A. has a proteinic natureB. decreases Ca-ions concentration in the bloodC. increases Ca-ions concentration in the bloodD. is secreted of the thyroid glandsE. is secreted of the parathyroid glands

44.5. 0,1,1,0,1Parathormone (parathyrin):A. has a steroidal natureB. is activator of hydroxylase in the liverC. 1,25-dihydroxycalciferol is needed for its actionD. 1,15-dihydroxycalciferol is needed for its actionE. increases absorption of Ca-ions in the intestine and kidneys

45.5. 0,1,1,1,0Calcitonin:A. is a hormone only of the parathyroid glandsB. is hormone of the thyroid and parathyroid glandsC. has an indirect mechanism of actionD. decreases Ca-ions concentration in the bloodE. increases Ca-ions concentration in the blood

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46.5. 1,0,0,1,0Hormones of the thyroid glands:A. are derivatives of amino acidsB. are derivatives of cholesterolC. thyroxine is an anabolic hormoneD. thyroxine is a catabolic hormoneE. thyroxine is triiodothyronine (T3)

47.5. 0,1,1,1,1Thyroxine and its characteristics:A. 3’,5’-cAMP is its secondary messengerB. albumins are its carriers in the bloodC. prealbumins are its carriers in the bloodD. a-globulins are its carriers in the bloodE. T4 has a higher affinity with proteins than T3

48.5. 1,1,1,1,1Metabolism of iodothyronines:A. aminotransferases use these hormones as substratesB. thyronine cycle is broken downC. they conjugate with UDP-glucuronic acidD. they conjugate with PAPSE. decarboxylases use thyronine-conjugates as substrates

49.5. 1,0,1,0,1Insulin:A. is secreted of b-cells of the Langerhans islandsB. is secreted of a-cells of the Langerhans islandsC. includes 51 amino acidsD. includes 84 amino acidsE. has 2 subunits

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50.5. 0,1,1,0,0Insulin:A. contains 3 S-S-bonds in its moleculeB. 2 S-S-bonds stabilize its quarternary structureC. quarternary structure includes a- and b-protomersD. quarternary structure includes a- and g-protomersE. contains 3 polypeptidic chains

51.5. 0,1,1,1,0Diabetes mellitus characteristics are:A. hypoglycemia, glucosuriaB. hyperglycemia, glucosuriaC. hyperglycemia, cetonemia, cetonuriaD. increases lypolysis and cetone bodies productionE. decreases lypolysis and cetone bodies production

52.5. 1,0,1,0,0Insulin:A. increases lipids synthesisB. decreases lipids synthesisC. increases glycolysisD. increases glycogen mobilizationE. decreases glycogen synthesis

53.5. 0,1,1,0,1Catecholamines are:A. synthetized in the cortex of medulla glandsB. synthetized in the medullaC. tyrosine derivativesD. tryptophan derivativesE. adrenalin, noradrenalin, dopamin

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54.5. 0,1,0,1,1Catecholamines:A. adrenalin via a-receptor activates production of 3’,5’-cAMPB. adrenalin via a-receptor activates production of 3’,5’-cGMPC. a-receptor is specific for adenylate cyclase systemD. a-receptor is specific for guanylate cyclase systemE. b-receptor is specific for adenylate cyclase system

55.5. 0,1,1,0,1Catecholamines:A. are vasodilatatorsB. are vasoconstrictorsC. increase blood pressureD. decrease blood pressureE. are inactivated by methylation and deamination

56.5. 1,0,1,1,1Glucocorticoids:A. are secreted from the cortex of medulla glandsB. are secreted from the medullaC. have cyclopenten-perhydrophenantren groupD. are pregnane derivativesE. are cholesterol derivatives

57.5. 1,0,1,1,0Glucocorticoids:A. are cortisol and corticosteroneB. are cortisol, corticosterone, aldosteroneC. are derivatives of cholesterolD. are pregnane derivativesE. have the membrane-cytosolic mechanism of action

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58.5. 0,1,0,0,1Glucocorticoids:A. decrease the glucose content in the bloodB. increase the glucose content in the bloodC. activate proteolysisD. inhibit lypolysisE. activate lypolysis

59.5. 0,1,1,1,0Glucocorticoids (GC):A. decrease the amino acids content in the bloodB. increase the amino acids content in the bloodC. transcortin is carrier of GCD. transcortin is synthetized in the liverE. transcortin is synthetized in the cortex of medulla glands

60.5. 1,0,1,0,0Glucocorticoids:A. increase proteins synthesis in the liver and kidneysB. decrease proteins synthesis in the liver and kidneysC. are activators of lympholysisD. are inhibitors of lympholysisE. are activators of urea synthesis and excretion

61.5. 0,1,0,1,1Characteristics of “steroid” diabetes (Icenko-Kushing disease):A. hypersecretion of glucocorticoidsB. hyposecretion of glucocorticoidsC. osteochondrosisD. osteoporosisE. blood pressure increases (hypertony)

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62.5. 1,0,1,0,1Characteristics of “steroid” diabetes:A. hyperglycemia and glucosuriaB. hypoglycemiaC. increases the amino acids content in the bloodD. the amino acids content in the blood decreasesE. aminoaciduria and ketonuria

63.5. 0,1,0,1,1Mineralocorticoids:A. are cortisol and corticosteroneB. are aldosterone and deoxycorticosteroneC. decrease Na-content in the bloodD. increase Na-content in the bloodE. increase Na and Cl content in the blood

64.5. 0,1,1,1,0Mineralocorticoids:A. are derivatives of tryptophanB. are derivatives of cholesterolC. have the cytosolic mechanism of actionD. increase reabsorption of NaClE. increase active transport (reabsorption) of H2O

65.5. 0,1,1,1,0Characteristics of hyperaldosteronism (Konn disease):A. hypotonia (decrease of blood pressure)B. hypertonia (increase of blood pressure)C. Na-content in the blood increasesD. K-content in the blood decreasesE. protein synthesis in the bones decreases

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66.5. 1,0,0,1,1Corticosteroids:A. cortisone is an effector of corticotropin (CTH)B. corticosterone is an effector of corticotropin (CTH)C. cytosol is a place for their synthesisD. mitochondria is the site for their synthesisE. pregnenolone is intermediate of corticosteroids synthesis

67.5. 0,1,1,0,1Sex hormones:A. are synthetized only in the sex glandsB. are synthetized in the sex glands and other tissuesC. have the cytosolic mechanism of actionD. have the membrane-cytosolic mechanism of actionE. are synthetized from cholesterol

68.5. 1,0,1,0,1Estrogens:A. contain 18 C-atoms in their structureB. contain 21 C-atoms in their structureC. are anabolic hormonesD. kidneys are the place of estrogens transformationE. liver is the place of estrogens transformation

69.5. 1,1,0,1,0Estrogens:A. are activators of RNA and proteins synthesisB. participate in phospholipids reconstructionC. don’t participate in phospholipids reconstructionD. increase Ca and phosphate content in the bloodE. decrease Ca and phosphate content in the blood

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70.5. 0,0,1,1,0Estrogens are:A. aldosteroneB. hydroxy-3-aldosteroneC. estradiolD. progesteroneE. testosterone

71.5. 1,0,1,0,1Male sex hormones:A. are androgensB. are estrogensC. is testosteroneD. have catabolic actionE. have anabolic action

72.5. 1,0,0,0,1Androgens:A. contain 19 C-atoms in their structureB. contain 21 C-atoms in their structureC. 3’,5’-cAMP is their secondary messengerD. 3’,5’-cGMP is their secondary messengerE. have the cytosolic mechanism of action

73.5. 0,0,1,0,1Androgens:A. decrease protein synthesisB. decrease DNA and RNA synthesisC. 17-ketosteroids are the end products of androgens catabolismD. 15-ketosteroids are the end products of androgens catabolismE. are used in the breast cancer therapy

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74.5. 0,1,1,0,1Prostaglandins:A. are hormonesB. are hormonoidesC. are used to decrease the blood pressure (hypertony therapy)D. are used to increase the blood pressure (hypotony therapy)E. arachidonic acid is a substrate of their synthesis

BLOOD: METABOLISM OF BLOOD CELLS, CHEMICALCOMPOSITION OF BLOOD PLASMA. BUFFER SYSTEMS OF

BLOOD. HEMOSTASIS

1.5. 1,0,1,0,1Blood functions are:A. transportB. catabolicC. bufferingD. catalyticE. hemostatic

2.5. 1,0,1,0,1Proteins of the blood are:A. albuminsB. prolaminsC. globulinsD. histonesE. lipoproteins

3.5. 1,0,1,1,0Enzymes of the blood are:A. alanyl aminotransferase (AlAT or GPT)B. hitinaseC. lactate dehydrogenase (LDH)D. acetylcholine esteraseE. uricase

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4.5. 1,0,0,1,1Nonproteinic nitrogenous compounds of the blood are:A. ureaB. cholesterolC. glucoseD. uric acidE. creatinine

5.5. 0,1,1,0,0Carbohydrates of the blood are:A. maltoseB. glucoseC. fructoseD. lactoseE. glycogen

6.5. 1,1,1,0,0Lipids of the blood are:A. cholesterolB. triacylglyceridesC. phospholipidsD. waxesE. acetone

7.5. 1,1,0,0,1Mineral components of the blood plasma are:A. Na+ (sodium)B. K+ (potassium)C. acetoneD. glycerolE. Cl- (chloride ions)

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8.5. 1,0,0,1,0Macroelements of the blood plasma are:A. NaB. MnC. CrD. KE. Se

9.5. 1,0,0,1,1Buffer systems of the blood are:A. bicarbonateB. arsenateC. glutamateD. phosphateE. proteinic

10.5. 1,0,0,1,1The correct statements about metabolic acidosis are:A. concentration of acids in the blood increasesB. concentration of urea in the blood increasesC. concentration of CO2 in the blood increasesD. concentration of ketone bodies in the blood increasesE. takes place in diabetes mellitus

11.5. 0,0,1,1,0Characteristics of gaseous alkalosis are:A. urea concentration in the blood increasesB. concentration of Ca-iones in the blood plasma increasesC. concentrations of Na and K-iones in the blood increasesD. concentration of CO2 in the blood decreasesE. concentration of Cl-iones in the blood plasma increases

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12.5. 1,0,0,1,0The correct statements about respyratory function of theblood:A. hemoglobin is the carrier of oxygenB. gaptoglobin is the carrier of oxygenC. oxyhemoglobin concentration in arteria blood is 67%D. oxyhemoglobin concentration in arteria blood is 97%E. carboxyhemoglobin is a complex of hemoglobin and CO2

13.5. 1,0,0,1,0Characteristics of hemoglobin forms:A. oxyhemoglobin is O2 transport form in the bloodB. carboxyhemoglobin is CO2 transport form in the bloodC. methemoglobin includes Fe2+

D. carbohemoglobin is a transport form of CO2E. oxyhemoglobin includes Fe3+

14.5. 0,0,1,1,0Carboanhydrase:A. is an enzyme for production of anhydrasesB. is only a leukocytic enzymeC. is an enzyme of H2CO3 decompositionD. has a high activity in the lungsE. is an enzyme of carbohemoglobin production

15.5. 1,0,0,1,0Characteristics of hemostatic function of the blood:A. fibrinogen is coagulating factor of the blood plasmaB. fibrinogen is the thrombocytic coagulating factorC. vitamin K is the blood plasma coagulating factorD. prothrombin (thrombinogen)is a nonactive factorE. prothrombin (thrombinogen)is an active factor

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16.5. 0,0,1,1,1Blood clotting factors are:A. fibrinolysinB. heparinC. fibrinogenD. thrombinE. Hageman

17.5. 1,1,0,0,1Natural anticoagulants are:A. fibrinolysinB. antithrombinC. pelentanD. sincumarE. heparin

18.5. 0,0,1,1,0Synthetic anticoagulants are:A. vikasolB. heparinC. pelentanD. dicumarinE. streptokinase

19.5. 1,0,0,1,0Procoagulants are:A. vitamin KB. vitamin B1C. plasminD. vitamin D3E. convertin

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20.5. 1,1,0,0,1Name pathology of the blood clotting:A. hemophiliaB. Christmas diseaseC. Edisson diseaseD. Hartnup diseaseE. Willebrand disease

21.5. 0,0,1,1,1Coagulating factors are:A. plasminB. adrenalinC. fibrinogenD. HagemanE. thrombin

22.5. 0,1,0,0,0Blood pH is:A. 7,38-7,48B. 7,36-7,44C. 7,42-7,49D. 7,32-7,48E. 7,30-7,45

23.5. 0,1,1,0,1Characteristics of metabolic acidosis:A. H2CO3 in the blood increasesB. pyruvate in the blood increasesC. hypercetonemiaD. urea content in the blood increasesE. lactate in the blood increases

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24.5. 0,0,1,0,1Characteristics of metabolic alkalosis:A. urea content in the blood increasesB. glutamine content in the blood increasesC. Cl-ions concentration in the blood decreasesD. Cl-ions concentration in the blood increasesE. Cl-ions excretion with urine increases

25.5. 0,1,0,0,0Ca2+ ions concentration in the blood plasma is:A. 2,12 - 3,45 mmol/LB. 2,25 - 2,75 mmol/LC. 3,25 - 3,75 mmol/LD. 2,55 - 2,85 mmol/LE. 3,65 - 4,35 mmol/L

26.5. 0,0,1,0,0Cl- ions concentration in the blood plasma is:A. 106 - 138 mmol/LB. 128 - 146 mmol/LC. 98 - 106 mmol/LD. 86 - 116 mmol/LE. 76 - 108 mmol/L

27.5. 1,1,0,0,1Factors of intrinsic mechanism of the blood coagulation (the 1st

stage) are:A. HagemanB. VIIIC. proconvertinD. VIIE. Stuart-Prauer

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28.5. 0,1,1,1,0Factors of extrinsic mechanism of the blood coagulation(the 1st stage) are:A. XIB. proconvertinC. VIID. Stuart-PrauerE. Rozental

29.5. 1,0,0,1,1CO2 transport forms in the blood:A. 3-5% in the blood plasma is a gasB. 1-3% in the blood plasma is a gasC. carboxyhemoglobin (10-15 %)D. carbohemoglobin (10-15%)E. NaHCO3

30.5. 0,1,0,1,0O2 transport forms in the blood:A. 3-5% in the blood plasma is a gasB. 2-3% in the blood plasma is a gasC. 1-2% in the blood plasma is a gasD. oxyhemoglobin (97-98%)E. oxyhemoglobin (87-89%)

31.5. 0,1,1,0,1Organospecific enzymes of the liver are:A. LDH3 and LDH4B. LDH5C. fructose-1-phosphate aldolaseD. fructose-1,6-diphosphate aldolaseE. alanine aminotransferase (AlATor GPT)

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32.5. 0,0,1,1,0Organospecific enzymes of the heart are:A. LDH2 and LDH3B. LDH3 and LDH4C. LDH1 and LDH 2D. aspartate aminotransferase (AsAT or GOT)E. alanine aminotransferase (AlAT or GPT)

33.5. 0,1,1,1,0Organospecific enzymes of the heart are:A. MM isoenzyme of CPK (creatine phosphokinase)B. MB isoenzyme of CPKC. LDH1D. AsAT (GOT)E. AlAT (GPT)

34.5. 0,0,1,1,1Organospecific enzymes of the liver are:A. creatine kinaseB. a-amylaseC. sorbitol dehydrogenaseD. ornithine carbamoyl transferaseE. histidase

35.5. 0,1,1,0,0Fe (ion) in the blood:A. Fe-content in the blood is 12-15 gB. Fe-content in the blood is 4,5-5,0 gC. the Fe2+ form is absorbed only in the small intestineD. the Fe3+ form is absorbed only in the small intectineE. hemoglobin contains about 50% of Fe

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BIOCHEMICAL INDICES

Chemical composition of blood plasma

I. Proteins

1. Total protein 65-85 g/L2. Albumins 35-50 g/L3. Globulins 25-35 g/L4. Fibrinogen 2.0-7.0 g/L5. Haptoglobin 0.28-1.90 g/L6. Prothrombin 10-15 mg/dL7. Plasminogen 1.4-2.8 mmol/L (20-40 mg/dL)8. Transferrin 19.3-45.4 mmol/L (170-400mg/dL)9. Ceruloplasmin 1.52-3.31 mmol/L ( 23-50 mg/dL)10. b-Lipoproteins 3.0-6.0 g/L (300-600 mg/dL)HDL – high density lipo-protein (a-LP)

1.063-1.210 mmol/L (80-400 mg/dL)

LDL – low density lipo-protein (b-LP)

1.006-1.063 mmol/L (360-640 mg/dL)

II. Enzymes

1. Alanyl aminotransferase (ALT)(glutamate pyruvate transferase,GPT)

0.16-0.68 mmol/h ×L or(15-75 IU/L)

2. Aspartate aminotransferase(AST) (glutamate oxaloacetatetransferase, GOT)

0.10-0.45 mmol/h × L or(10-50 IU/L)

3. Lactate dehydrogenase 0.8-4.0 mmol/h × L4. Creatine kinase < 1.2 mmol/h × L or (< 90 IU/L)5. Fructose-biphosphate aldolase(F-1,6-PA)

3.6-21.8 mmol/h × L

6. Acetylcholine esterase 160-340 mmol/ h × L

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7. a-Amylase 15-30 g/h × L or (< 300 IU/L)

8. Alkaline phosphatase 30-150 IU/L9. Acidic phosphatase < 62 nkat/L10. g-Glutamyl transferase (gGT or GGT) < 60 IU/L

Nonproteinic nitrogenous compounds

1. Nitrogen residual (nonpr-oteinic)

19.5-30.0 mmol/L

2. Nitrogen of amino acids 3.5-5.5. mmol/L3. Creatine 15-70 mmol/L4. Creatinine 60-150 mmol/L5. Urea 3.3-6.7 mmol/L6. Uric acid 0.1-0.4 mmol/L7. Bilirubin total 8-20 mmol/L8. N-Acetylneiraminic acid 1.8-2.2 mmol/L9. Histamine 17.99-71.94 nmol/L(0.2-0.8 mg/dL)10. Adrenalin 1.91-2.46 nmol/L (0.35-0.45 mg/L)11. Serotonine 0.3-1.7 mmol/L (5.0-30.0 mg/dL)12. Thyroxine 64.36-141.59 nmol/L (5-11mg/dL)

III. Carbohydrates and metabolites

1. Glucose 2.8-6.0 mmol/L2. Lactate 0.5-2.0 mmol/L3. Pyruvate < 0.1 mmol/l4. Citric acid 88.5-156.1 mmol/L (1.7-3.0 mg/dL)

IV. Lipids and metabolites

1. Total lipids 4.0-8.0 g/L2. Triacylglycerides 0.5-2.1 mmol/L3. Total phospholipids 2.0-3.5 mmol/L4. Total cholesterol 4.0-8.6 mmol/L

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5. Free fatty acids 0.3-0.8 mmol/L6. Ketone bodies 100-600 mmol/L

V.Mineral components

1. Sodium (Na+) 135-155 mmol/L2. Potassium (K+) 3.6-5.0 mmol/L3. Chlorides (Cl-) 97-108 mmol/L4. Calcium (Ca2+) 2.25-2.75 mmol/L5. Phosphate inorganic 0.8-1.4 mmol/L6. Magnezium (Mg2+) 0.7-1.0 mmol/l7. Sulphates 0.4-0.6 mmol/L8. Iron (Fe) 14-32 mmol/L (65-175 mg/dL)9. Copper (Cu) 12-19 mmol/L10. Zinc (Zn) 12-20 mmol/L11. Ammonia 10-47 mmol/L

Indices of blood

1. Hemoglobin: malesfemales

130-180 g/L (13-18 g/dL)120-160 g/L (12-16 g/dL)

2. Hydrogen ion: arterial blood 35-46 nmol/L (pH= 7.36-7.44)(38o C)

3. Oxygen (Po2) in arterial blood: 11-15 kPa ( 85-105 mm Hg)4. Bicarbonate total (CO2) 22-30 mmol/L5. Carbon dioxide (Pco2) inarterial blood:

4.5-6.0 kPa (35-46 mm Hg)

Indices of urine

Density (r) 1.017-1.020pH 5.7-6.5Urea 220-609 mmol/24 h (20-35 g/24 hCreatinine 7.1-17.7 mmol/24 h ( 0.8-2.0 g/24 hUric acid 1.60-3.54 mmol/24 h ( 270-600 mg/24 h)

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Indican 46.0-56.4 mmol/24 hCalcium (Ca2+) 2.50-6.25 mmol/24 h ( 100-250 mg/24 h)Cloride ion (Cl-)Ketone bodies: acetoneacetoacetic acid

400-600 mg/L100-200 mg/L

Chondroitine sulphates 2.7-7.5 mg/24 hPyruvic acid 113.7-283.9 mmol/24 h (10-25 mg/24 h)Uropepsinogen 150-300 IU/24 h (1.5-3.0 mg/24 h)a-Amylase (diastase): 1.0-2.0 IU/ml (100-200 IU/dL) Volgemut’s method: 16-64 IU/LAdrenalin < 13.3 mg/24 hNoradrenalin < 79.8 mg/24 h17-ketosteroids: malesfemale

42.48-46.75 mmol/24 h (12.83±0.8 mg/24 h)34.78-39.16 mmol/24 h (10.61±0.66 mg-/24 h)

Indices of saliva

Daily volume (V) 500-1500 ml (500-1500 ml/24 h)pH 6.07-7.9Density (r) 1.08-1.32

Nitrogen-contaning organic substances

Proteins 1.4-6.4 g/LMucine 0.8-6.0 g/LAmmonia 0.01-0.12 g/LUrea 0.14-0.75 g/LUric acid 0.005-0.029 g/LCreatinine 0.005-0.750 g/LCholine 0.005-0.036 g/L

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Nitrogen-noncontaning organic substances

Glucose 0.10-0.30 g/LCitric acid < 0.020 g/LLactic acid 0.01-0.05 g/LCholesterol 0.025-0.500 g/L

Inorganic substances

Sodium (Na) 5.2-24.4 mmol/LPotassium (K) 14-41 mmol/LCalcium (Ca) 2.3-5.5 mmol/LChlorides (Cl-) 15.1-31.6 mmol/LPhosphate inorganic 0.080-0.217 g/LBicarbonate (HCO3

-) 2.13-13.00 mmol/LFluor (F-) 0.8-2.5 g/LBrom (Br-) 0.2-7.1 mg/LTiocianate (SCN-) 0.12-0.33 g/LMagnezium (Mg2+) 0.16-1.06 mmol/lSulphates 0.04-0.2 g/LCopper (Cu) 0.5-7.6 mg/LZinc (Zn) 0.06-0.80 g/LVitaminesThiamine (B1) 0.7 mg/dLRiboflavin (B2) 5.0 mg/dLPyridoxine (B6) 60 mg/dLNicotinic acid (PP) 3.0 mg/dLPantotenic acid 8.0 mg/LAscorbic acid (C) 0.58-3.78 mg/LBiotin (H) 0.08 mg/dLPhyllochinon (K) 1.5 mg/Dl

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LITERATURE

1. Bhagavan N.V. Medical Biochemistry. Fourth Edition,Academic Press, 2002.

2. Campbell P.N., Smith A.D. Biochemistry illustrated. Inter-national Edition, 2000.

3. Dati Francesco, Metzman Erwin. Proteins. Laboratory tes-ting and clinical use. Includes index. Holzheim, Germany, 2005.

4. Dawson Rex M.C., Elliott Daphne C., Elliott William H.,Jones Kenneth M. Data for Biochemical Research. Third Edition.Clarendon Press, Oxford, 1986.

5. Emery A.E.H., Mueller R.F. Elements of Medical Genetics.ELBS Longman Group UK Ltd., 1992.

6. Marshall William J. Clinical Chemistry. Fourth edition,2000.

7. Metzler D.E. Biochemistry. The chemical reactions of li-ving cells. Second Edition, vol. 1-2. Academic Press, 2003.

8. Murray R.K., Granner D.K., Mayes P.A., Rodwell V.W.Harper’s illustrated Biochemistry. Twenty-Sixth edition. Interna-tional Edition, 2003.

9. Nelson D.L., Cox M.M. Lehninger principles of Bioche-mistry. 3-rd Edition p.cm. Includes index, 2000.

10. Russel P.J. Genetics, 3rd Edition. Harper Collins Publi-schers, New York, 1992.