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Tver State Medical University

Department of Biochemistry with Clinical Laboratory Diagnostic

Tests for Biochemistry

Teaching manual for foreign students

Second edition

Tver 2018

УДК 577.1

ББК 52.57

Authors:

D.V.Leshchenko, assistant Professor, PhD in Biology

M.B.Belyakova, assistant Professor, PhD in Biology

V.V.Zhigulina, assistant Professor, PhD in Biology

I.V.Namestnikova, assistant Professor, PhD in Medicine

E.N.Egorova, Doctor of Medicine, MD

The reviewers:

Assistant Professor of the department of Biology TSMU N.V.Kostiuk, PhD in Biology

Assistant Professor of the department of Chemistry TSMU N.P.Lopina, PhD in Chemistry

Tests for Biochemistry [Текст]: Teaching manual for foreign students / D.V.Leshchenko, M.B.Belyakova, V.V.Zhigulina, I.V.Namestnikova, E.N.Egorova. - Tver. – TSMU. – 2018. – p. 100.

The foreign students of 2 course can use tests for self-preparation for routine monitoring and examination in biochemistry. Tests can be used by teachers in a theoretical part of lessons for students’ training in biochemistry.

© Department of Biochemistry with Clinical Laboratory Diagnostic,2018

Content:

I. I topic. Structure and functions of proteins …………………………….…4

II. II topic. Chemistry, functions of enzymes and vitamins. Biochemistry of nutrition. Biological oxidation…………………..……………..…………..11

III. III topic. Metabolism and functions of carbohydrates..……………… .31

IV. IV topic. Metabolism and functions of lipids………………………… .41

V. V topic. Metabolism of proteins……………………………………….. 55

VI. VI topic. Special biochemistry of organs and tissues………………… 66

VII. Correct answers………………………………………………………..91

VIII. Literature………. ……………………………………………….……96

I. ASSIGNMENTS IN THE TEST FORM

I.1. Topic 1. Structure and functions of proteins

Select one or more correct answers

1.NEGATIVE CHARGED AMINO ACIDS ARE

1) proline

2) lysine

3) glutamic acid

4) aspartic acid

5) valine

2.THE TERTIARY STRUCTURE OF THE PROTEIN IS

1) sequence of amino acids in the polypeptide chain

2) spatial laying of the secondary structure of the protein

3) spatial laying which is due to the only by ionic bonds

4) organization of the proteins from several polypeptide chains

5) all mentioned is right

3.AMINO ACIDS HAVING AN ACIDIC property

1) alanine

2) leucine

3) glutamic acid

4) lysine

5) aspartic acid

4.PRIMARY STRUCTURE OF THE PROTEIN IS

1) connection of amino acids in the polypeptide chain with covalent bond -CO-NH-

2) nucleic acids chain

3) formation of a-spiral

4) polymer chain is made of amino acid residues connected by peptide bonds

5) structure consisting of subunits

5.SELECT THE STATEMENTS CHARACTERIZING PROTEINS

1) they have a common formula Cn(H2O)m

2) they contain residues of 40 or more amino acids

3) they contain residues of less than 40 amino acids

4) they contain Nitrogen

5) they contain peptide bonds

1) 6.PROTEINOGENIC AMINO ACIDS ARE

2) α-amino acids

3) β-amino acids

4) γ-amino acids

5) L - isomers of amino acids

6) D - isomers of amino acids

7.CHOOSE HYDROPHOBIC AMINO ACIDS

1) aspartic acid

2) arginine

3) alanine

4) threonine

5) triptophan

8.SELECT THE ACIDIC AMINO ACID

1) aspartate

2) arginine

3) alanine

4) threonine

5) triptophan

9.ALBUMINS PERFORM THE FOLLOWING FUNCTIONS

1) transport of O2

2) transport of fatty acids

3) formation of humoral immunity

4) formation of oncotic pressure

5) providing hemostatic function

10.SOLUBILITY OF PROTEINS DEPENDS ON

1) molecular mass of the protein

2) presence of hydrophobic amino acids in the structure

3) value of pH of the solution

4) value of the charge

5) forms of the protein molecule

11.ISOELECTRIC POINT OF THE PROTEIN (SELECT THE RIGHT ANSWERS)

1) certain value of pH in the solution at which the protein molecule is electro neutral

2) it depends on the primary structure of the protein

3) it depends on molecular mass of the protein

4) it depends on conformation of the protein molecule

5) it depends on pH of the solution

12.DENATURATION OF THE PROTEIN IS CHARACTERIZED BY

1) loss of native properties

2) destruction of all structural levels of the protein

3) peptide bonds are present

4) protein sediments

5) excretion of hydrophobic groups on outer surface of the protein molecule

13.AN ISOELECTRIC POINT IS CHARACTERIZED BY

1) the protein easily falls out into sediments

2) solubility of the protein increases

3) destruction of the primary structure of the protein

4) positive and negative charges in the protein molecule are the same

5) proteins lose their ability to move in the eclectic field

14.CHOOSE THE RIGHT STATEMENTS ABOUT SALTING OUT OF PROTEINS

1) proteins fall out into sediments under the influence of neutral salt solutions

2) proteins sediment under the influence of heavy metal salts

3) proteins preserve solubility

4) the loss of the protein primary structure

5) proteins partly lose hydration shell and the charge on the globular surface

15.ISOELECTRIC POINT (IEP) OF THE GLUTAMIC ACID

1) IEP >7

2) IEP<7

3) IEP=7

4) in acidic medium

5) in basic medium

16.ISOELECTRIC POINT OF LYSINE

1) IEP >7

2) IEP<7

3) IEP=7

4) in acidic medium

5) in basic medium

17.PROSTHETIC GROUP OF HEMOGLOBIN IS

1) mg-porphyrine

2) heme which contains trivalent iron (ferric iron)

3) heme which contains divalent of iron

4) heme which contains iron with changeable valency

5) formylporphyrine

18.CHOOSE THE PHOSPHOPROTEINS

1) caseinogen

2) active phosphorylase

3) active glycogensynthase

4) insulin

5) chymotrypsin

19.PROSTHETIC GROUP OF HEMOPROTEINS IS

1) mg-porphyrines

2) heme

3) derivatives of vitamin B2


5) derivates of vitamin A

20.PRESENCE OF EVERY PROTEIN IN SOLUTION CAN BE DETERMINED BY REACTION

1) biuret reaction

2) xanthoproteic

3) ninhydrin reaction

4) with phenylisothiocyanate

5) foll`s reaction

21.FOR QUANTITATIVE DETERMINATION OF AMINO ACIDS IN SOLUTION IT IS USED

1) biuret reaction

2) xanthoproteic

3) foll`s reaction

4) ninhydrin reaction

5) sakaguchi reaction

22.FOR THE REMOVAL OF LOW-MOLECULAR SUBSTANCES FROM PROTEINIC SOLUTIONS IT IS USED THE METHOD OF

1) electrophoresis

2) affine chromatography

3) dialysis

4) ultracentrifugation

5) salting out

23.FUNCTION OF ALBUMINES

1) oxygen transport

2) transportation of fatty acids

3) formation of humoral immunity

4) formation of cell immunity

5) hemostatic function

24.WHAT FRACTION OF PROTEINS OF BLOOD SERUM IS RELATED TO IMMUNE PROTEINS

1) albumins

2) alpha-globulins

3) beta-globulins

4) gamma-globulins

5) all mentioned is right

25.BLOOD PROTEINS ARE NOT THE PROTEINS

1) albumins

2) histones

3) globulins

4) fibrinogen

5) hemoglobin

26.TRANSPORT OF СО2 FROM TISSUES TO LUNGS is realized by

1) xyhemoglobin

2) carbhemoglobin

3) methemoglobin

4) aminohemoglobin

5) deoxyhemoglobin

27.nucleotide is differeD from nucleoside becouse of it

1) has a secondary structure

2) contains phosphate residues

3) contains purine bases

4) contains pyrimidine bases

5) contains pentose

28.structural PART OF CHROMATIN IS NOT

1) DNA

2) RNA

3) histones

4) non-histone proteins

29.TYPES OF RNA are DIFFERENT by

1) primary structure

2) molecular weight

3) nucleotide sequence

4) functions in the cell

5) all of the above is true

30.POST-TRANSLATION MODIFICATION OF PROTEINS CAN BE THROUGH

1) phosphorylation

2) hydroxylation

3) partial proteolysis

4) covalent binding with prosthetic group

5) all of the above is true

31.PLASMATIC MEMBRANES OF CELLS ARE DIFFERED BY

1) lipid composition

2) amount of proteins

3) amount of cholesterol

4) protein composition

5) all answers are correct

32.MEMBRANE HAS

1) asymmetry

2) the mosaic arrangement of proteins

3) lipid bilayer

4) cholesterol


33.COMPONENTS OF THE CHROMATIN ARE

1) DNA

2) RNA

3) histones

4) hyaluronic acid

5) non-histone proteins

34.ACTIVATION OF AMINO ACIDS AND FORMATION OF AMINOACYL-T-RNA TAKE PLACE AT THE PARTICIPATION OF THE FOLLOWING ENZYMES

1) DNA polymerase

2) RNA polymerase

3) aminoacyl-t-RNA-synthetase

4) nuclease

5) ligase

35.THE PROCESS OF REPLICATION INCLUDES

1) formation of Okazaki fragments

2) unspiralization of DNA

3) usage of GTP, ATP, UTP, CTP

4) polymeryzation of DNA

5) usage of DNA ligase

36.FOR THE FORMATION OF THE INITIATIVE COMPLEX AT PROTEINS BIOSYNTHESIS THE FOLLOWING COMPONENTS ARE NECESSARY

1) 30S and 50S ribosomal subunits

2) m-RNA

3) n- formylmethionine-TRNA

4) factors of initiation (IF-1, IF-2, IF-3), GTP, Mg2+

5) initiating codon of mRNA

37.IN THE SYNTHESIS OF RNA THE FOLLOWING components TAKE PART

1) operon

2) DNA polymerase

3) DNA dependent RNA polymerase

4) DNA ligase

5) d-ATP, d-GTP, d-CTP, d-TTP

38.HIV INFECTION IS DETECTED BY THE PRESENCE IN THE BLOOD

1) antibodies to HIV

2) antigens of HIV

3) DNA provirus

4) ketone bodies

5) bilirubin

39.CHEMICAL PROCESSES AFTER THE INFECTION OF HIV IN THE HUMAN ORGANISM ARE

1) interaction of the virus with glycoproteins on the surface of host cellular membranes

2) joining of the virus and host cell membranes. Penetration of the capsule with the virus genome into the cell

3) release of nucleoid of virus genomic RNA

4) synthesis of provirus DNA on the matrix of virus genomic RNA with the help of reverse transcriptase

5) including of the genomic provirus DNA into the genome (DNA) of the host cell

40. THE COMMON FEATURE FOR NATIVE AND FOR DENATURATED RYBONUCLEASE ARE

1) primary structure

2) conformation

3) structure of active center

4) interradical bonds

5) function

41.ERYTHROMYCIN BINDS 60S SUBUNIT OF RIBOSOME AND INHIBITS

1) translation in human cells

2) maturation of rna

3) translation in bacterial cell

4) transcription in bacterial cell

5) posttranslational modification of proteins

42.INTERFERONS

1) have protein nature

2) are produced in response to viral infection

3) activate rnaase which splits rrna

4) cause stoppage of protein synthesis in infected cells

5) damage structure of small subunit of ribosome

43.DIFFERENCE IN PROTEIN COMPOSITION OF VARIOUS TISSUES IS EXPLAINED BY THAT

1) in different tissues different genes are expressed

2) genome of various cell is different

3) genes of proteins, absent in the tissue, are permanently repressed

4) expression of genes are controlled by mechanisms of adaptive

induction and repression

5) permanently repressed genes are not activated by factors of inner and external medium

44.MUTATIONS CAN APPEAR IN RESULT OF

1) modification of nitrogen base in dna molecule

2) replace of nucleotide in dna consequence

3) insertion of deoxyribonucleotides in dna chain

4) deamination of residues of adenine and cytosine in rna

5) formation of thymine dimers in dna strands

45.ENHANCER IS

1) DNA site which can bind regulatory protein and stimulate

transcription

2) DNA-binding regulatory protein

3) non-transcribed 5'-end site of DNA

4) transcription factor, binding RNA-polymerase

5) gene, coding the protein, regulating the transcription

I .2. Topic 2. Structure, function of enzymes and vitamins. Biochemistry of nutrition. Biological oxidation

46.THE ACTIVE CENTER OF ENZYMES IS (CHOOSE THE MOST COMPLETE ANSWER)

1) the center of the substrate binding

2) allosteric centre

3) group of amino acids located consequently in the polypeptide chain

4) catalytic center + binding substrate centre

5) allosteric center + centre with joining substrate

47. MECHANISM OF ENZYMES ACTIVITY INCLUDES

1) distribution of electron density of substrate chemical bonds

2) decrease of activation energy

3) binding the substrate with the enzyme active center

4) formation of new chemical bonds in molecules under the influence of the enzyme

5) separation of enzymes in initial (unchanged) form

48. PROSTHETIC GROUP OF THE ENZYME IS

1) apoenzyme spiral

2) radicals of aminoacids

3) coenzymes or cofactors

4) ions of metals

5) protein part of the enzyme

49. FACTORS INFLUENCING THE ENZYME REACTION RATE

1) concentration of the enzyme

2) concentration of the substrate

3) pH

4) temperature

5) inhibitors (activators) influence

50.. THE COMPETITIVE INHIBITION OCCURS WHEN THE INHIBITOR

1) has the similar chemical structure with the substrate

2) decreases the quantity of es-complex

3) binds the allosteric enzyme centre

4) changes primary enzyme structure

5) acts irreversibly

51. IN OPPOSITE TO THE INORGANIC CATALYSTS THE ENZYMES ACT AT

1) temperature of 25 -37º c

2) temperature of 100º c

3) high pressure

4) normal pressure

5) neutral pH

52.THE CHROMOPROTEINS WITH ENZYME ACTIVITY ARE

1) pepsin

2) trypsin

3) chymotrypsin

4) peroxidase

5) catalase

53.INTERNATIONAL CLASSIFICATION OF ENZYMES DIVIDES THEM INTO 6 CLASSES IN ACCORDANCE WITH THEIR

1) structure

2) substrate specificity

3) activity

4) the type of catalyzing reaction

5) organ specificity

54.THE ENZYMES WITH ABSOLUTE SPECIFICITY ARE

1) pepsin

2) lipase

3) urease

4) amylase

5) arginase

55. THE REACTIONS CATALYZED BY THE ENZYMES OF THE LIGASE CLASS

1) oxidation-reduction reactions

2) isomerization

3) intermolecular transport of different radicals and atoms

4) rupture of c-o, c-c, c-n bonds and reversible reactions of different substrate groups splitting from substrates hydrolytically

5) synthesis of organic substances from two initial molecules using atp energy

56.LACTATE DEHYDROGENASE BELONGS TO THE CLASS OF

1) oxidoreductases

2) transferases

3) hydrolases

4) ligases

5) isomerases

57.PEPSIN BELONGS TO THE CLASS OF

1) oxidoreductases

2) transferases

3) hydrolases

4) ligases

5) isomerases

58.IN COMPETITIVE INHIBITION THE INHIBITOR BINDS WITH

1) allosteric centre

2) active centre

3) enzyme coding genome

4) enzyme-substrate complex

5) substrate

59.THE MULTIENZYME COMPLEX IS

1) lactate dehydrogenase

2) synthetase hfa

3) pepsin

4) trypsin

5) hexokinase

60.INTERNATIONAL UNIT OF ENZYME ACTIVITY (E) IS THE ENZYME QUANTITY WHICH AT OPTIMAL CONDITIONS CATALYSES

1) 1 mMol of the substrate in 1min

2) 1 mMmol of the substrate in 1 sec

3) 1 mkMmol of the substrate in 1 min

4) 1 mkMmol of the substrate in 1 sec

5) 1 mole of the substrate in 1 min

61.ENZYME CATALYZING THE REACTIONS OF INTERMOLECULAR TRANSFER OF DIFFERENT ATOMS BELONGS TO THE CLASS OF

1) oxidoreductases

2) transferases

3) hydrolases

4) ligases

5) isomerases

62.ENZYMES HAVE PROPERTIES

1) amphoteric

2) electrophoretical mobility

3) ability to dialysis (they pass through semipermeable membrane)

4) low viscosity

5) high diffusion rate

63.LACTATE DEHYDROGENASE CONTAINS

1) two type of subunits

2) four type of subunits

3) two subunits

4) four subunits

5) five subunits

64.COMPOUND (CONJUGATED) ENZYMES (APOENZYME+COFACTOR) ARE

1) pepsin

2) trypsin

3) chymotrypsin

4) peroxidase

5) catalase

65.ENZYMES, CATALYZING SPLITTING OF INORGANIC SUBSTANCE INTRAMOLECULAR BONDS WITH the HELP OF WATER, BELONG TO CLASS

1) oxidoreductases

2) transferases

3) hydrolases

4) lyases

5) ligases

66.COFACTOR FUNCTION CAN BE EFFECTED BY

1) lipoic acid

2) ATP

3) Mo2+

4) sulfuric acid

5) Ca2+

67.ENZYMES INCREASE THE RATE OF REACTION BECAUSE

1) they change free energy of the reaction

2) they decrease the rate of reverse reaction

3) they change equilibrium of the reaction

4) they decrease activation energy

5) they selectively increase the rate of direct reaction but do not increase the rate of reverse reaction

68.IT IS RECOMMENDED TO DETERMINE THE ACTIVITY OF ENZYME UNDER CONDITIONS OF

1) short time after reaction starting

2) substrate concentration less then km

3) buffer system with optimal ph

4) temperature 25-300 c

5) saturation by substrate

69.DETECT THE TYPE OF TRANSFORMATIONS which are CATALYZED BY KINASES

1) transfer group within the molecular

2) cleavage c-c bonds

3) transfer phosphate group from donor molecular onto acceptor

4) accepting of water

5) elimination or accepting of electrons

70.AMP TAKES PART IN CHEMICAL COMPOSITION OF COENZYMES

1) tiamine diphosphate (TDP)

2) biotin

3) NAD

4) FMN

5) FAD

71.AMINO GROUP IS TRANSFERRED BY COENZYME

1) TDP

2) FMN

3) pyridoxal phosphate

4) biotin

5) HS-CoA

72.SIMILARITY OF ENZYMES AND INORGANIC CATALYSTS

1) catalyze direct and reverse reaction

2) characterized by high specificity

3) denaturated at high temperature

4) consumed during the reaction

5) increase the energy of activation

73.IN FORMATION OF ACTIVE CENTRE OF ENZYME THEY TAKE PART

1) α-amino groups of amino acids

2) α-carboxylic group of amino acids

3) imino groups of peptide bonds

4) functional groups of amino acids` radicals

5) carbonylic groups of peptide bonds

74.MICHAELIS CONSTANT CHARACTERIZES

1) affinity of enzyme to substrate

2) activity of enzyme

3) affinity to coenzyme

4) affinity to cofactor

5) affinity to inhibitors

75.ENZYMES, SYNTHESIZED IN FORM OF INACTIVE PRECURSORS

1) amylase

2) pepsin

3) trypsin

4) aminopeptidase

5) chymotrypsin

76.ENZYME that has GROUP SUBSTRATE SPECIFICITY is

1) arginase

2) trypsin

3) glutamate dehydrogenase

4) succinate dehydrogenase

5) histidase

77.COENZYMES, TAKING PART IN DEHYDROGENATION REACTIONS

1) FAD

2) CoA

3) biotin

4) NAD


78.COENZYMES, PARTICIPATE IN OXIDATIVE DECARBOXYLATION OF Α-KETOACIDS


2) NADP+

3) biotin

4) TPP

5) THFA

79.DIISOPROPYLFLUOROPHOSPHATE IRREVERSIBLY INHIBITS


2) cytochrome oxidase

3) acetylcholinesterase

4) folate dehydrogenase

5) malate dehydrogenase

80.”CATAL” HAS UNITS

1) μM/min

2) m/sec

3) mM/min

4) mM/sec

5) μM/sec

81.OPTIMAL SPECTRUM OF ENZYMES, USED FOR ENZYMODIAGNOSTIC OF MYOCARDIUM INFARCT

1) α-amylase, lipase

2) creatine kinase, aldolase

3) GPT, cholinesterase

4) aldolase, lipase

5) LDH1, GOT, CK

82.THE RATE OF ENZYMATIC REACTION DEPENDS ON

1) enzyme concentration

2) substrate concentration

3) pH, temperature

4) the effect of inhibitors (activators)


83.LACTATEDEHYDROGENASE BELONGS TO CLASS

1) oxidoreductases

2) transferase

3) hydrolase

4) ligase

5) isomerase

84.Pepsin BELONGS to enzymes cleaving

1) lactose

2) triglycerides

3) proteins

4) phospholipids

5) starch

85.IN COMPETITIVE INHIBITION THE INHIBITOR BINDS WITH

1) allosteric center

2) active center

3) the gene encoding the enzyme

4) enzyme-substrate complex

5) substrate

86.The enzymes that digest protein, do not belong

1) pepsin

2) trypsin

3) chymotrypsin

4) catalase

5) collagenase

87.ENZYMES INCREASE THE RATE of A REACTION BECOUSE OF THEY

1) increase the rate of the reverse reaction

2) reduce the rate of the reverse reaction

3) alter the reaction equilibrium

4) reduce the energy of activation

5) selectively increase the rate of direct reaction, but do not increase the rate of the reverse reaction

88.COENZYMES PARTICIPATING IN DEHYDROGENASE REACTIONS

1) biotin, thiamine diphosphate

2) biotin, coenzyme A

3) FAD, NAD

4) NAD, pyridoxal phosphate

5) FAD, pyridoxal phosphate

89.ISOENZYMES

1) catalyze both direct and reverse reactions

2) catalyze the transformation of substrates of similar structure

3) catalyze the same reaction, but differing in their physico-chemical properties

4) belong to the isomerase class

5) are enzymes of the same class

90.MIXTURE OF TWO OR SEVERAL ENZYMES CANNOT BE SEPARATED BY THE METHOD OF

1) dialysis

2) gel filtration

3) salting out

4) electrophoresis

5) ion exchange chromatography

91.HYDROGEN PEROXIDE IS DECOMPOSED BY THE ENZYME

1) oxygenase

2) hydroxylase

3) peroxidase

4) cytochrome oxidase

5) cytochrome reductase

92.REGULATION OF ENZYMES ACTIVITY IN THE HUMAN ORGANISM IS HAPPENED BY

1) hydrolysis of peptide bonds (partial proteolysis)

2) phosphorylation/dephosphorylation

3) separation of regulatory subunits from catalytic

4) attachment of the effector to the allosteric center


93.THE RATE OF ENZYMATIC REACTION IS INCREASED AT

1) increasing of temperature over 450С

2) increasing of enzyme concentration

3) acute change of pH

4) addition of an inhibitor

5) enzyme denaturation

94.PROSTHETIC GROUP OF RETINAL-PROTEINS PROVIDING VISION IS

1) Mg-porphyrines

2) heme



5) derivatives of vitamin A

95.VITAMIN, PARTICIPATING IN OXIDATIVE DECARBOXYLATION OF THE PYRUVIC ACID

1) vitamin A

2) vitamin B1

3) vitamin K

4) vitamin PP

5) vitamin B2

96.VITAMIN B6 TAKES PART IN

1) transport of protons and electrons in the respiratory chain

2) oxidative deamination of amino acids

3) transamination

4) hydroxylation of phenylalanine

5) decarboxyalation of amino acids

97.PELLAGRA IS CAUSED BY THE DEFICIENCY OF VITAMIN

1) tocopherol

2) nicotinamide

3) folic acid

4) vitamin C

5) vitamin K

98.SHOW THE BIOCHEMICAL DISORDERS CAUSED BY THE DEFICIENCY OF VITAMIN K

1) change of phosphor-calcium exchange

2) disturbance of collagens biosynthesis

3) disturbance of blood coagulation factors synthesis

4) decrease in the level of opsin in retina

5) disturbance in synthesis of purine nucleotides

99.CALL THE VITAMINS SYNTHESIZED BY THE INTESTINE MICROFLORA

1) ascorbic acid

2) vitamin D

3) folic acid

4) biotin

5) vitamin B12

100.SHOW BIOCHEMICAL DISORDERS CAUSED BY THE DEFICIENCY OF VITAMIN D

1) inhibition of redox reactions

2) disturbance of bone tissue mineralization

3) disturbance of blood coagulation factors synthesis

4) disturbance in absorption of Ca2+ and P3+ in GIT

5) increased excitability of nervous tissue

101.VITAMIN C IS USED FOR THE TREATMENT OF SUCH DISEASES AS

1) beriberi

2) pellagra

3) diabetes mellitus

4) scurvy

5) night blindness

102.BIOLOGICAL ROLE OF THE PANTOTHENIC ACID IS

1) a part of NAD-dependent dehydrogenases

2) a part of coenzyme A

3) a part of FAD-dependent dehydrogenases

4) participating in light perception processes

5) necessary for normal blood coagulation

103.CALL THE VITAMIN, WHICH IS AN ANTIOXIDANT

1) vitamin B1

2) vitamin B6

3) vitamin D

4) vitamin E

5) vitamin K

104.BIOLOGICAL ROLE OF THE FOLIC ACID

1) takes part in the reactions of dehydrogenation

2) takes part in the reaction of Krebs cycle

3) takes part in the purine bases synthesis

4) takes part in the process of tissue respiration

5) takes part in decay process

105.NAME THE DISEASE OR CLINICAL SYMPTOMS, ASSOCIATED WITH THE DEFICIENCY OF VITAMIN B2

1) glossitis

2) cataract

3) rickets

4) scurvy

5) pellagra

106.NAME THE DISEASE OR CLINICAL SYMPTOMS, ASSOCIATED WITH THE DEFICIENCY OF VITAMIN A

1) rickets

2) night blindness

3) xerophthalmia

4) scurvy

5) delayed growth

107.THE ABSENCE OF WHICH VITAMIN MAY LEAD TO CREATINE SYNTHESIS DISORDER

1) B9 (folic acid)

2) C (ascorbic acid)

3) B1 (thiamine)

4) B2 (riboflavin)

5) B5 (nicotine acid)

108.NAME THE VITAMINS REFERRED TO WATER-SOLUBLE GROUP

1) vitamin A

2) vitamin E

3) vitamins of B-group

4) ascorbic acid

5) vitamin K

109.GIVE ALL NAMES OF VITAMIN A

1) antixerophthalmic

2) antihemorrhagic

3) retinol

4) tocopherol

5) rutin

110.GIVE ALL NAMES OF VITAMIN B1

1) thiamine

2) folic acid

3) antidermatitic

4) antineuritic

5) lipoic acid

111.WHICH VITAMIN HAS COBALT (Co2+)

1) thiamine

2) riboflavin

3) vitamin B12

4) nicotinamide

5) vitamin B6

112.CALL THE VITAMIN SYNTHESIZED FROM CHOLESTEROL

1) vitamin K

2) vitamin B3

3) vitamin D

4) vitamin B1

5) vitamin H

113.VITAMIN B1 TAKES PART IN THE NEXT REACTIONS

1) in the oxidative decarboxylation of pyruvate

2) in a reaction of transamination

3) in the oxidative decarboxylation of a-ketoglutarate

4) in the transketolase reaction of pentose phosphate pathway

5) in the fatty acids’ biosynthesis

114.VITAMIN, PARTICIPATING IN COENZYME A FORMATION, IS

1) para-Amino-benzoic acid (PABA)

2) pyridoxine

3) carnitine

4) orotic acid

5) pantothenic acid

115.VITAMIN, PARTICIPATING IN THE REACTIONS OF CARBOXYLATION, IS

1) thiamine

2) riboflavin

3) biotin

4) pantothenic acid

5) folic acid

116.VITAMINS, PARTICIPATING IN THE REACTION OF TRANSMETHYLATION, ARE

1) vitamin P

2) vitamin F

3) vitamin B12

4) vitamin B9

5) vitamin B15

117.VITAMIN, WHICH INFLUENCES ON CAPILLARY PERMEABILITY IS

1) nicotinamide

2) riboflavin

3) pyridoxine

4) rutin

5) pangamic acid

118.VITAMIN, COMPONENT OF FAD

1) ascorbic acid

2) pantothenic acid

3) folic acid

4) riboflavin

5) nicotinic acid

119.VITAMIN, COMPONENT OF TPP (TDP)

1) biotin

2) thiamine

3) pyridoxine

4) riboflavin

5) ascorbic acid

120.SHOW ALL NAMES OF VITAMIN D3

1) antirachitic

2) antihemorrhagic

3) tocopherol

4) cholecalciferol

5) retinol

1) 121.VITAMIN, COMPONENT OF METHYLCOBALAMIN

2) В1

3) В2

4) В3

5) В12

6) В5

122.NAME VITAMIN – PRECURSOR OF COENZYME, HARTICIPATING IN DECARBOXYLATION OF AMINO ACIDS

1) biotin

2) riboflavin

3) thiamine

4) cobalamin

5) pyridoxine

123.NAME VITAMIN WHICH HAS ROLE OF COENZYME, NECESSARY FOR MATURATION OF COLLAGEN

1) pantothenic acid

2) folic acid

3) ascorbic acid

4) nicotinic acid

5) riboflavin

124.NAME PROVITAMIN A

1) keratin

2) carotene

3) creatine

4) carnitine

5) carnosine

125.RICKETS IS RESULT OF INSUFFICIENCY OF VITAMIN

1) tocopherol

2) vitamin D

3) folic acid

4) vitamin B12

5) ascorbic acid

126.AS COENZYME, PYRIDOXAL PHOSPHATE PARTICIPATES IN REACTIONS

1) redox

2) isomerization

3) transacylation

4) carboxylation

5) transamination

1) 127.NAME VITAMIN, DEFICIENCY OF WHICH CAUSES BERI-BERI

2) В2

3) В1

4) В3

5) В6

6) В5

128.ENZYMES OF RESPIRATORY CHAIN CARRY OUT OXIDATION BY

1) dehydrogenation

2) transport of electrons

3) transport of protons

4) reduction of oxygen

5) inclusion of oxygen in substrate

129.OXIDATIVE PHOSPHORYLATION

1) synthesis of atp linked with usage of energy of electron transport in respiratory chain

2) synthesis of atp linked with usage of macroergic substrates

3) synthesis of atp connected with usage of o2

4) synthesis of atp catalyzed by atp synthetase

5) synthesis of atp in glycolytic reaction

130.TRANSPORT OF ELECTRONS AND OXIDATIVE PHOSPHORYLATION OCCURS IN

1) in the cytoplasm of the cell

2) on the inner membrane of mitochondria

3) on the outer membrane of mitochondria

4) in the mitochondrial matrix

5) in the nucleic membrane

131.MICROSOMAL OXIDATION IS A USE OF O2 (OXYGEN)

1) in the bioenergetic process

2) in the plastic purpose

3) for the oxidation of steroid hormones

4) for the oxidation of xenobiotics

5) for the oxidative stage of detoxification of putrefactive products in liver

132.OXIDATIVE PHOSPHORYLATION IS INHIBITED BY

1) 2,4-dinitrophenol

2) cyanide

3) puromycin

4) antimycin -A

5) thyroxin

133.MICROSOMAL SYSTEM OF OXIDATION INCLUDES

1) NADPH2

2) flavoproteids

3) Fe-protens

4) NADH2

5) cytochrome P450

134.ACTIVE PART OF NAD-DEPENDENT DEHYDROGENASE CONTAINS

1) vitamin B3

2) vitamin PP

3) vitamin B12

4) nyacine

5) vitamin H

135.THE MAIN RESPIRATORY CHAIN CONTAINS

1) cytochrome

2) flavoproteins

3) ubiquinone

4) Fe - Proteins

5) NADP – depended dehydrogenase

136.SEQUENCE OF ENZYMES` LOCALIZATION IN RESPIRATORY CHAIN IS DETERMINED BY

1) redox potential

2) concentration of oxygen

3) value of pH

4) oxidation / reduction potential

5) are arbitrary

137.ORIGINS OF ACETYL-COA ARE

1) ADP

2) glucose

3) amino acids

4) urea

5) pyruvate

138.INDICATE THE POSITIONS, WHICH ARE CHARACTERIZED BY BIOLOGICAL SIGNIFICANCE OF TCA CYCLE

1) oxidation of acetyl-CoA with the formation of 2 molecules of CO2, 1 GTP, 3 NADH2, 1 FADH2

2) oxidation of acetyl CoA with the help of oxaloacetate

3) oxidation of glucose up to the pyruvate

4) oxidation of glucose up to lactate

5) formation of α-ketoacids

139.INDICATE CARBOXYLIC ACIDS WHICH ARE DONATORS OF REDUCED COENZYMES IN RESPIRATORY CHAIN

1) citrate

2) isocitrae

3) acetic acid

4) fumaric acid

5) malate

140.CHOOSE AMOUNT OF ATP THAT ARE FORMED BY SUBSTRATE PHOSPHORYLATION AT COMPLETE OXIDATION OF ACETYL-COA IN krebs CYCLE

1) 1 molecule

2) 30 molecules

3) 10 molecules

4) 12 molecules

5) 15 molecules

141.NAME NUTRIENTS WHICH DOESN’T TAKE PART IN THE INHIBITION OF LIPIDS’ FREE RADICAL OXIDATION IN THE HUMAN ORGANISM

1) carotenoids

2) tocopherol

3) ascorbic acid

4) pantothenic acid

5) glutathione

142.DETECT THE PROCESS WHICH IS CONNECTED WITH MITOCHONDRIAL FORMS OF HYPOENERGETIC CONDITION

1) deficiency of O2 in air

2) destruction of mitochondrial membranes’ integrity

3) disturbance of blood circulation

4) insufficiency of vitamins B1, B2, PP

5) action of uncouplers of respiration and phosphorylation

143.THE INCREASE OF WHAT SUBSTANCES IN MITOCHONDRIA ACCELERATES THE REACTIONS OF COMMON PATHWAY OF METABOLISM

1) pyruvate

2) NADH2

3) ADP

4) FADH2

5) citrate

144.THE CONCENTRATION OF WHAT SUBSTANCES INCREASES IN MITOCHONDRIA AT REDUCING OF OXYGEN CONSUMPTION

1) pyruvate

2) NADH2

3) AMP, ADP

4) Ca 2+

5) NAD

145.CHOOSE KEY ENZYMES OF CITRIC ACID CYCLE

1) citrate synthetase

2) malate dehydrogenase

3) isocitrate dehydrogenase


5) α-ketoglutarate dehydrogenase

146.CHOOSE ENZYMES CATALYZING THE REACTION WHICH DIRECTLY LINKED WITH ATP BIOSYNTHESIS

1) ATP-synthetase

2) NADH-dehydrogenase

3) QH- dehydrogenase

4) NAD-depended dehydrogenase

5) cytochromoxydase

147.METABOLISM IS THE COMPLEX OF REACTION IN WHICH OCCURS

1) breakdown of organic molecules to CO2 and H2O in the cells

2) transformation of energy of organic molecules into energy of macroergic bonds of ATP

3) synthesis of structural and functional compounds of the cells

4) converting biopolymers of foods into unspecific substances

5) usage of energy of catabolic processes for functional activity of organism

148.DETECT SENTENCE WHICH IS CORRECT FOR MECHANISM OF OXIDATIVE PHOSPHORYLATION

1) transport of protons occurs through inner mitochondrial membrane towards mitochondrial matrix in the process of functioning of electrons transport chain

2) energy of organic molecules transforms into energy of proton electrochemical potential

3) unidirectional transport of protons towards intermembrane space leads to protons gradient

4) protonophors (uncouplers) uncouples respiration and phosphorylation

5) energy of electrochemical potential is used for atp biosynthesis

149.THE ATP↔ADP CYCLE INCLUDES (CHOOSE THE MOST

FULL ANSWER)

1) use of energy of chemical bonds of ATP for work

2) ATP synthesis with the help of energy of nutrients oxidation

3) useage of ATP for various types of work and the regeneration of ATP at catabolic reactions

4) substrate phosphorylation

5) hydrolysis of high-energy bonds of ATP with heat production

150.THE COMMON PATHWAY OF PROTEINS, LIPIDS AND CARBOHYDRATES CATABOLISM INCLUDES

1) urea production cycle

2) Krebs cycle

3) glycolysis

4) oxidative decarboxylation of pyruvate

5) penthose phosphate pathway of glucose oxidation

151.DONATOR OF HYDROGEN FOR COMPLEX II OF RESPIRATORY CHAIN IS

1) succinate

2) citrate

3) alanine

4) succinyl-CoA

5) aspartate

152.CARBON MONOXIDE (CO)

1) uncoupler of oxidative phosphorylation and ETC

2) inhibitor of succinate dehydrogenase

3) activator of free-radical oxidation

4) inhibitor of NADH-dehydrogenase

5) inhibitor of cytochromoxidase

153.VALUE P/O ≤ 2 AT OXIDATION OF

1) malate

2) isocitrate

3) α-ketoglutarate

4) succinate

5) pyruvate

154.INCLUSION OF OXYGEN INto MOLECULE OF SUBSTRATE IS CATALYZED BY

1) dehydrogenases

2) reductases

3) deaminases

4) oxygenases

5) lyases

155.HYDROGEN PEROXIDE IS SUBSTRATE FOR

1) superoxide dismutase

2) NADP-oxidase

3) glutathione reductase

4) catalase

5) NADH-oxidase

156.REDUCING EQUIVALENTS (NADH OR FADH) ARE FORMED IN THE REACTION OF

1) oxidative decarboxylation of α-ketoglutarate

2) hydration of fumarate

3) formation of succinyl-CoA

4) transformation of citrate into isocitrate

5) synthesis of citrate

157.UNCOUPLERS OF OXIDATIVE PHOSPHORYLATION

1) inhibit enzymes of ETC

2) inhibit enzymes of TAC

3) transport H+ across membrane against proton gradient

4) inhibit H+-ATPase

5) transfer protons from intermembrane space into mitochondrial matrix beside proton channel

158.COMMON PRODUCT OF BOTH MICROSOMAL AND MITOCHONDRIAL OXIDATION

1) ATP

2) endogenic water

3) NADP

4) NADH

5) FADH

159.THE VALUE P/O≤3 AT OXIDATION OF SUBSTRATE UNDER THE ACTION OF

1) NAD-dependent dehydrogenase

2) cytochrome P450

3) monoamine oxidase

4) dioxygenase

5) FAD-dependent succinate dehydrogenase

160.UBIQUINONE PROVIDES ELECTRON TRANSPORT BETWEEN COMPLEXES

1) I and II

2) I and IV

3) III and IV

4) IV and V

5) I and III

161.MACROERGIC COMPOUNDS ARE

1) succinyl-CoA

2) ATP

3) creatine phosphate

4) phosphoenolpyruvate


162.CHOOSE AN ENZYME CATALYZING REACTION DIRECTLY CONNECTED WITH ATP SYNTHESIS IN MITOCHONDRIA


2) FAD-dependent dehydrogenase

3) QH-dehydrogenase

4) Cytochrome oxidase

5) ATP synthase

163.COMMON CATABOLIC PATHWAY OF PROTEINS, LIPIDS AND CARBOHYDRATES INCLUDES

1) urea cycle

2) Krebs cycle

3) glycolysis

4) gluconeogenesis

5) pentose-phosphate pathway of glucose oxidation

164.RESPIRATORY CHAIN ENZYMES INCLUDE

1) calcium

2) iron

3) phosphorus

4) cobalt

5) fluorine

165.ATP-SYNTHETASE

1) is located in the inner mitochondrial membrane

2) performs the synthesis of ATP

3) is activated by H+

4) consists of several protomers


166.NAME ALL FINAL PRODUCTS OF CATABOLISM

1) water

2) carbon dioxide

3) urea

4) ammonia


I .3. Topic 3. Metabolism and functions of carbohydrates

167.GLYCOPROTEINS TAKE PART IN THE FOLLOWING BIOLOGICAL PROCESSES

1) construction of the cellular membrane

2) immunological reactions

3) transport of iron (Fe)

4) transport of copper (Cu)

5) adhesion of cells

168.FUNCTIONS OF CARBOHYDRATES AND THEIR DERIVATIVES ARE

1) energetic

2) receptor

3) protective

4) antitoxic (UDPGA)

5) structural

169.NAME CARBOHYDRATES OF THE HUMAN FOOD WHICH ARE THE SOURCES OF GLUCOSE AT DIGESTION

1) sucrose

2) lactose

3) starch

4) cellulose

5) glycogen

170.ON ACUTE PANCREATITIS THE DIAGNOSTIC TEST IS

1) increased activity of α-amylase in urine

2) decreased activity of α-amylase in urine

3) increased activity of α-amylase in blood

4) decreased activity of α-amylase in blood

5) increased activity of pancreatic lipase in blood

171.IN GLYCOGEN DISINTEGRATION UP TO GLUCOSE (GLYCOGENOLYSIS) THE FOLLOWING SUBSTANCES TAKE PART

1) liver phosphorylase

2) glucose-6-phosphatase of skeletal muscles

3) inorganic phosphate

4) phosphorylase of muscles

5) glucose-6-phosphatase of the liver

172.DETECT THE MECHANISM OF GLUCOSE PENETRATION FROM THE INTESTINAL LUMEN INSIDE THE INTESTINAL WALL

1) simple diffusion

2) endocytosis

3) facilitated diffusion

4) simport

5) antiport

173.CARBOHYDRATES WHICH SHOULD BE EXCLUDED FROM THE FOOD AT HEREDITARY FRUCTOSE INTOLERANCE ARE

1) lactose

2) sucrose

3) maltose

4) mannose

5) starch

174. DETECT THE ENZYME, PARTICIPAING IN DIGESTION OF CARBOHYDRATES IN GASTRO-INTESTINAL TRACT

1) amylase

2) sucrase

3) lactase

4) trypsin

5) maltase

175.REACTIONS OF GLYCOGEN BIOSYNTHESIS FROM GLUCOSE ARE CATALYZED BY

1) cholesterol esterase

2) glycogen phosphorylase

3) glycogen synthetase

4) phosphoglucomutase

5) hexokinase

176.SOURCES of THE GLUCOSE in BLOOD ARE

1) glycogen of the liver

2) carbohydrates of the food

3) glycogenic amino acids

4) higher fatty acids

5) lactate

177.IN REACTIONS OF GLYCOGEN SYNTHESIS FROM GLUCOSE THE FOLLOWING NUCLEOSIDE TRIPHOSPHATES ARE USED

1) АТP

2) GТP

3) UТP

4) CТP

5) ТТP

178.GLYCOGEN MOBILIZATION WITH THE SUBSEQUENT GLUCOSE realizing INTO THE BLOOD OCCURS IN

1) myocardium

2) skeletal muscles

3) the liver

4) the brain

5) erythrocytes

179. CHOOSE THE IRREVERSIBLE REACTIONS OF GLYCOLYSIS

1) aldolase

2) pyruvate kinase

3) phosphofructokinase

4) hexokinase


180.CHOOSE THE CORRECT DESCRIPTION OF ANAEROBIC GLYCOLYSIS

1) it provides energy to skeletal muscles at first minutes of urgent intensive work

2) it activates in myocardium at blood supply disturbance and hypoxia

3) it is the main source of energy for erythrocytes metabolism

4) it provides АТP synthesis by substrate phosphorylation

5) it promotes blood рН maintenance at the constant level

181.GLUCOSE-6-PHOSPHATE IS FORMED AS A RESULT OF

1) phosphoglucomutase action on glucose-1-phosphate

2) fructose-6-phosphate isomerization under the action of hexose phosphate isomerase

3) hexokinase action on glucose

4) glycogen splitting under the phosphorylase action

5) reactions between glucose and АТP at presence of glucokinase

182.THE MAIN BIOLOGICAL SIGNIFICANCE OF PENTOSE-PHOSPHATE PATHWAY IS

1) its intermediates are includes in aerobic and anaerobic glycolysis

2) production of NАDPН2 in cell cytoplasm, supply of pentoses (mainly by ribose-5-phosphate) for synthesis of nucleotides

3) synthesis α-ketoacids

4) oxidation of acetyl-CoA up to СО2 and Н2О

5) formation of lactate

183.DETERMINE AMOUNT OF АТP MOLECULES WHICH ARE PRODUCED AT OXIDATION OF D-GLUCOSE MOLECULE UP TO LACTATE

1) 3

2) 4

3) 2

4) 6

5) 8

184.THE END PRODUCT OF ANAEROBIC GLYCOLYSIS IS

1) pyruvate

2) lactate

3) phosphoenolpyruvate

4) ethanol

5) acetyl-CoA

185.NAME ENZYMES PARTICIPATING IN THE PROCESS OF GLUCONEOGENESIS

1) glucose-6-phosphatase

2) fructose bisphosphatase

3) pyruvate kinase

4) phosphoenolpyruvate carboxykinase

5) phosphorylase

186.GLUCONEOGENESIS MAINLY TAKES PLACE IN

1) liver

2) myocardium

3) erythrocytes

4) fat tissue

5) kidneys

187.NAME ENZYMES THAT ARE ACTIVATED AT HYPOGLYCEMIA

1) glucose-6-phosphatase in the liver


3) phosphorylase in the liver

4) phosphorylase of muscular tissues

5) enzymes of gluconeogenesis

188.GLUCOSURIA AT DIABETES MELLITUS IS CAUSED BY

1) hyperglycemia

2) increased glycogen disintegration in the liver and muscles

3) activation of gluconeogenesis

4) abnormal filtration ability of kidneys

5) decreased renal permeability level

189. KETONURIA AT DIABETES MELLITUS IS A CONSEQUENCE OF

1) increased ketogenesis in the liver

2) inappropriate reabsorption of ketone bodies in kidneys

3) disoders in oxidation of ketone bodies by skeletal muscles

4) hyperketonemia

5) increasing of ketone bodies recycling in skeletal musculature

190.HYPERGLYCEMIC COMA AT DIABETES MELLITUS IS CHARACTERIZED BY

1) hyperglycemia

2) ketose

3) hyperosmolarity

4) glucosuria

5) decreased glucose level in insulin-dependent tissues

191.METABOLIC ACIDOSIS AT DIABETES MELLITUS IS A CONSEQUENCE OF ACCUMULATION IN THE BLOOD THE FOLLOWING SUBSTANCES

1) acetone

2) acetoacetate

3) β-hydroxybutyrate

4) glucose

5) citric acid

192.THE MAIN BIOLOGICAL ROLE OF PENTOSE PHOSPHATE PATHWAY

1) a source of NADPH2

2) in there reaction ketone bodies are formed

3) formation of pentose for nucleotide’s biosynthesis

4) formation of reduced coenzymes for the reaction of reduction

5) the intermediates of this pathway are used for glucose biosynthesis

193.AGLYCOGENOSIS ARE HEREDITARY DISEASES WITH FOLLOWING FEATURES

1) it is a result of glycogen synthetase defect

2) very low supply of glycogen in the liver and other tissues of patient

3) hypoglycemia in postabsorptive state

4) morning convulsions are outstanding characteristics of this disease

5) the disease is compatible with life, but ill children need hourly alimentation

194.THE MAIN PROCESS WHICH USE ATP IN THE HEPATOCYTES IS

1) transmembrane transport of substances

2) synthesis of protein

3) synthesis of glycogen

4) synthesis of lipids

5) gluconeogenesis

195.THE MAIN SUBSTRATE OF GLUCONEOGENESIS ARE

1) pyruvate

2) lactate

3) glycerol

4) glucogenic amino acids

5) acetyl-CoA

196.THE CHILD OF 2 YEARS OLD HAS VOMITING, DIARRHEA, A PAIN IN STOMACH AFTER EATING AS A RESULT OF INFECTION OF GIT. EXCLUSION OF MILK FROM MEAL RESULTS TO DISAPPEARANCE OF THESE SYMPTOMS. CHOOSE A REASON OF THE DISEASE

1) hereditary defect of pancreatic amylase

2) hereditary defect of saccharase

3) hereditary defect of lactase

4) acquired defect of lactase

5) acquired defect of saccharase

197.BIOLOGICAL ROLE OF LACTATE IS

1) it can uses for formation of essential amino acids

2) it is a fuel for heart work by transformation into pyruvate

3) it forms in erythrocytes always

4) it uses for glucose formation in the gluconeogenesis

5) it is dehydrogenized with NADH2 and pyruvate formation

198.INCREASING OF LACTATE LEVEL IN THE BLOOD CAN BE AS A RESULT OF

1) deficiency of vitamin B1

2) deficiency of enzymes of TCA

3) intensive physical work

4) inhibiting of enzymes of electron transport chain


199.PHOSPHORYLATION IS A VARIANT OF ACTIVATION FOR ENZYME

1) adenylate cyclase


3) kinase of phosphorylase

4) proteinkinase during mobilization of glycogen

5) glycogen phosphorylase b

200.THE PRODUCT OF AEROBIC GLYCOLYSIS IS

1) CO2

2) H2O

3) lactate

4) pyruvate

5) acetyl-CoA

201.CHOOSE THE CORRECT SENTENCES FOR GLYCEROL-3-PHOSPHATE SHUTTLE MECHANISM

1) the oxidation nadh2 to nad is occurs in the process of converting dihydroxyaceton phosphate to glycerol-3-phosphate

2) glycerol-3-phosphate, which formed in this process, is transported across mitochondrial membrane

3) glycerol-3-phosphate is a donor of electro and proton for FAD-dehydrogenase

4) synthesis of 2 molecules of ATP is possible by substrate phosphorylation

5) glycerol-3-phosphate shuttle mechanism is acted in muscle cells

202.THE METABOLITES WHICH ARE USED FOR AMINO ACIDS, LIPIDS, GLUCOSE, DNA, RNA BIOSYNTHESIS ARE

1) pyruvate

2) 3-phosphoglycerate

3) keton bodies

4) acetyl-CoA

5) phosphoribosyl pyrophosphate

203.DISACCARIDE, CONSISTING OF GALACTOSE AND GLUCOSE, IS

1) lactose

2) isomaltose

3) sucrose

4) maltose

5) starch

204.HYDROLYSIS OF SUCROSE IN GIT OCCURS IN

1) mouth cavity

2) stomach

3) small intestine

4) large intestine

5) duodenum

205.ENZYME, CATALYZING THE REACTION OF SUBSTRATE PHOSPHORYLATION IN THE GLYCOLYSIS

1) hexokinase

2) aldolase

3) pyruvate kinase


5) phosphofructokinase

206.NAME MACROERGIC SUBSTANCES OF GLYCOLYSIS

1) glyceraldehyde 3-phosphate

2) 1,3 -bisphosphoglycerate

3) pyruvate

4) 2-phosphglycerate

5) phosphoenol pyruvate

207.NAME THE PROCESS IN WHICH ENZYMES ACT IN THE ORDER: HEXOKINASE, PHOSPHOGLUCOSE ISOMERASE, PHOSPHOFRUCTOKINASE

1) glycogen synthesis

2) glycogen mobilization

3) gluconeogenesis

4) pentose phosphate pathway

5) glycolysis

208. NAME THE PROCESS IN WHICH ENZYMES ACT IN THE ORDER: HEXOKINASE, PHOSPHOGLUCOMUTASE, GLUCOSE-1-PHOSPHATE URIDYL TRANSFERASE


2) glycogen mobilization

3) gluconeogenesis


5) glycolysis

209.SHOW MISSED METABOLITE OF GLYCOLYSIS: 2-PHOSPHOGLYCERATE → PHOSPHOENOL PYRUVATE→ ? → LACTATE

1) 3-phosphglycerate

2) dihydroxyacetone phosphate

3) fructose-1,6-bisphosphate

4) pyruvate

5) glyceraldehyde-3-phosphate

210. SHOW MISSED METABOLITE OF GLYCOGEN MOBILIZATION GLYCOGEN→ ? → GLUCOSE-6-PHOSPHATE → GLUCOSE

1) glucose-1-phosphate

2) fructose-6-phosphate

3) fructose-1,6-bisphosphate


5) glyceraldehyde-3-phosphate

211.MALATE-ASPARTATE SHUTTLE ACTS IN ORGANS

1) skeletal muscles

2) liver

3) kidney

4) brain

5) heart

212.DEFICIENCY OF WHICH ENZYME CAUSES FRUCTOSURIA

1) hexokinase

2) 6-phosphofructokinase

3) phosphoglucose isomerase

4) glucose-6-phosphatase

5) fructokinase

213.GLUCONEOGENESIS IS

1) aerobic glucose oxidation

2) anaerobic oxidation of glucose

3) synthesis of glucose from non-carbohydrate components


5) glycogen degradation

214.METABOLIC ACIDOSIS AT DIABETES MELLITUS IS CONNECTED WITH ACCUMULATION IN THE BLOOD

1) glucose, glucose 6-phosphate

2) oxaloacetate, malate

3) malate, succinate

4) acetoacetate, β-hydroxybutyric acid

5) glycerol, glycerol-3-phosphate

215.THE MAIN SUBSTRATE OF GLUCONEOGENESIS IS

1) acetone

2) pyruvate

3) acetoacetate

4) β-hydroxybutyric acid

5) succinate

216.LACTATE IS CHARACTARIZED BY

1) formation at anaerobic conditions

2) conversion to pyruvate

3) formation in erythrocytes

4) usege for glucose synthesis at gluconeogenesis


217.INCREASING OF LACTATE CONCENTRATION IN THE BLOOD TAKE PLACE AT

1) increased physical activity

2) lack of vitamin C

3) lack of vitamin D

4) lack of vitamin A

5) lack of vitamin K

218.GLYCOGEN IS

1) monosaccharide

2) disaccharide

3) protein

4) homopolysaccharide

5) lipid

219.HEPARIN IS

1) monosaccharide

2) amino acid

3) protein

4) phospholipid

5) heteropolysaccharide

220.CAUSE OF GLYCOGENOSIS IS

1) disoder of triglycerides synthesis

2) disoder of purine synthesis

3) disoder of glycogen degradation

4) disoder of glucose degradation

5) lack of enzymes of the Krebs cycle

221.CAUSES OF AGHYLOGENOSIS ARE

1) disoder of triglycerides synthesis

2) disoder of purine synthesis

3) disoder of glycogen synthesis

4) disoder of glucose degradation

5) lack of enzymes of the Krebs cycle

222.α-amylase cleaves

1) polypeptides

2) phospholipids

3) starch

4) sucrose

5) triglycerides

223.NAME A POLYSACCHARIDE OF NATURAL ORIGIN THAT CAN BE USED as ANTICOAGULANT

1) glycogen

2) chitin

3) heparin

4) chondroitin sulfate

5) keratan sulfate

224.THE MOST RELIABLE CAUSE OF PAIN IN MUSCLE AFTER INTENSIVE PHYSICAL WORK IS

1) enhanced muscle protein breakdown

2) creatinine accumulation

3) lipid reduction

4) accumulation of lactic acid

5) increasing the content of ADP

225.AMOUNT OF ATP THAT IS FORMED DURING GLUCOSE OXIDATION UP TO CO2 AND H2O

1) 2-4

2) 12-14

3) 20-22

4) 30-32

5) 36-38

IV. IV topic. Metabolism and functions of lipids

226.THE FUNCTIONS OF LIPIDS ARE THE FOLLOWING

1) are structural components of cell membranes

2) form of energy storage

3) precursors of steroid hormones

4) carry genetic information

5) are main source for the production of macroergs

227.FULL HYDROLYSATE OF GLYCEROPHOSPHOLIPIDS CONTAINS (CHOOSE THE FULLEST ANSWER)

1) glycerol and fatty acids

2) glycerol, fatty acids, phosphoric acid

3) glycerol, fatty acids, phosphoric acid and nitrogen bases

4) glycerol, fatty acids and nitrogen bases

5) glycerol, fatty acids, phosphoric acid and glucose

228.CHOOSE MORE CORRECT STATEMENTS CHARACTERIZING LIPIDS

1) general formula Cn(H2O)m

2) during hydrolysis forms acetylCoA

3) non-soluble in polar solvents

4) they are often complex esters of fatty acids and alcohols

5) they are natural polymers

229. POLYUNSATURATED FATTY ACIDS WITH MORE THAN TWO DOUBLE BONDS

1) enter the structure of complex lipids

2) precursors of eicosanoids ( prostaglandins)

3) source of energy

4) precursors of carbohydrates

5) transport the hydrophilic hormones

230.THE FORMULA OF PALMITIC ACID IS

1) C14

2) C16

3) C16:1

4) C16:2

5) C20:4

231.DETECT THE PAIRS OF LIPIDS WHICH HAVE DIRECT OPPOSITE BIOLOGICAL ACTIVITY

1) prostaglandins and leucotriens

2) cholic and litocholic acid

3) thromboxane TXA2 and prostacyclin (PGI2)

4) acetoacetate and β-hydroxybutyrate

5) acetone and β-hydroxybutyrate

232.DETECT THE STATEMENT WHICH DESCRIBE PHOSPHOGLYCERIDES

1) they are amphipathic

2) they are formed from glycerol-3-phosphate

3) cell membranes contain them

4) they are the most important storage of energy

5) they contain two residues of fatty acids

233. BILE ACIDS CARRY OUT

1) emulsification of fats

2) decrease of the surface tension in the boundary of division fat/water

3) increase of the surface tension in the boundary of division fat/water

4) stabilization of formed emulsion

5) helps to absorb fats

234.RESYNTHESIS OF TRIGLYCERIDES IN THE INTESTINAL WALL OCCURS WITH PARTICIPATION OF

1) monoglyceride

2) active forms of fatty acids

3) acyl-CoA

4) acetyl-CoA

5) HS-CoA

235.MAIN TRANSPORT FORM OF ENDOGENIC CHOLESTEROL TO THE TISSUES

1) chylomicrons

2) LDL

3) VLDL

4) HDL

5) non-etherified fatty acids

236.ACTIVATION OF PROLIPASE AND LIPASE TAKES PLACE WITH THE PARTICIPATION OF

1) colipase

2) pepsin

3) bile acids

4) trypsin

5) phospholipids

237.THE PLACE OF LIPIDS RESYNTHESIS

1) liver cells

2) intestinal wall

3) fatty tissue

4) kidneys

5) CNS

238.LIPOPROTEIN LIPASE CARRIES OUT

1) hydrolysis of lipids in the intestine

2) hydrolysis of triglycerides in fatty tissue

3) hydrolysis of lipoproteins complex in the blood

4) hydrolysis of triglycerides in the liver

5) hydrolysis of phospholipids in membranous structure

239.THE MECHANISM OF ASSIMILATION OF LIPIDS BY THE ORGANISM CELLS FROM LIPOPROTEINS INCLUDES

1) hydrolysis of lipoproteins by lipoproteinlipase

2) endocytosis

3) emulsification of lipids

4) forming of cholesterol ester with the help of LCAT

5) interaction of lipoproteins with cell membranes receptors

240.MOBILIZATION OF LIPIDS IS

1) hydrolysis of lipids in the intestine

2) hydrolysis of lipids in lipoproteins

3) hydrolysis of lipids in fatty tissue

4) hydrolysis of lipids in the liver

5) biosynthesis of lipids in fat tissue

241.FATTY ACIDS, FORMED DURING THE MOBILIZATION OF LIPIDS, ARE TRANSPORTED BY THE BLOOD WITH THE HELP OF

1) chylomicrons

2) VLDL

3) LDL

4) HLDL

5) albumin

242.MOBILIZATION OF LIPIDS REGULATED BY

1) hormones

2) trough the adenylate cyclase system

3) by changing of the activity of monoglyceridlipase

4) by changing of the activity of diglyceridlipase

5) by changing of the activity of triglyceridlipase

243.AT (-OXIDATION OF FATTY ACIDS THE FOLLOWING SUBSTANCES PARTICIPATE IN THE REACTION OF DEHYDROGENATION

1) HS-CoA

2) NAD

3) FAD

4) acyl-CoA-dehydrogenase

5) acyl-CoA

244.SYNTHESIS OF KETONE BODIES GOES THROUGH THE FORMATION STAGE OF:

1) phosphatidic acid

2) diacylglyceride

3) b-hydroxy-b-methylglutaryl-CoA

4) glycerol-3-phosphate

5) mevalonic acid

245.DURING (-OXIDATION IN THE SECOND REACTION OF DEHYDRATION THE FOLLOWING SUBSTANCES PARTICIPATE

1) FA

2) carnitine

3) NAD


5) thiolase

246. CALL THE STAGES OF OXIDATION OF HIGH FATTY ACIDS

1) activation of fatty acids

2) oxidative decarboxylation

3) β-oxidation

4) oxidation of acetyl-CoA in the Krebs cycle

5) transport of acetyl-CoA from mitochondria to cytoplasm

247.ENERGY VALUE OF 1 CYCLE OF (-OXIDATION

1) 2 ATP

2) 3 ATP

3) 4 ATP

4) 5 ATP

5) 7 ATP

248.OXIDATION OF FATTY ACIDS WITH THE ODD NUMBER OF CARBON ATOMS

1) doesn’t differ from the oxidation of higher fatty acids with even number of carbon atoms

2) passes through the formation of propionyl-CoA

3) passes through the formation of succinyl-CoA

4) needs the participation of the vitamins biotin and B12

5) needs the participation of thiamin

249.SPLITTING OF TWO CARBON FRAGMENTS ATOMS FROM ACYL-COA INCLUDES FOUR REACTIONS. THE FOLLOWING ONES WHICH DESCRIBE THE SEQUENCE OF REACTIONS MORE CORRECTLY ARE

1) oxidation, dehydratation, reduction, splitting

2) reduction, dehydratation, reduction, splitting

3) dehydrogenation, hydratation, dehydrogenation, splitting

4) hydration, dehydratation, hydration, splitting

5) reduction, hydratation, dehydration, splitting

250.OXIDATION of unsaturated fatty acids is characterized by

1) forming of propionyl-CoA

2) forming of succinyl-CoA

3) forming of trans-isomers from cys-isomers

4) gives 2 ATP more than the oxidation of saturated fatty acids

5) gives 2 ATP less than the oxidation of saturated fatty acids

251.KETONE BODIES INCLUDE

1) acetone

2) acetoacetate

3) β-oxybutyrate

4) acetate

5) oxaloacetate

252.BIOLOGICAL ROLE OF KETONE BODIES

1) are the main energetic substrate for the liver

2) are energetic substrate for muscles

3) move pH of the blood to acidosis

4) are a transport form of acetyl-CoA

5) are used for glucose biosynthesis

253.MAIN WAYS OF REMOVING CHOLESTEROL FROM THE HUMAN Body ARE

1) way of oxidation up to CO2 and H2O

2) with sweating from the skin

3) with the bile as bile acids

4) oxidation till the steroid hormones and after inactivation they are discharged with the urine

5) in unchanged structure with the urine

254.TRANSPORT OF CHOLESTEROL FROM THE ORGANS AND TISSUES TO THE LIVER IS MADE BY

1) chylomicrons

2) VLDL

3) LDL

4) HDL

5) albumin

255.LECITIN-CHOLESTEROL-ACYLTRANSFERASE (LCAT)

1) is placed in HDL

2) is placed in VLDL

3) provides the formation of cholesterol ethers

4) is necessary for transfer of cholesterol from cells and LDL into HDL

5) is necessary for transfer of cholesterol from HDL in LDL and cells

256.TOTAL AMOUNT OF ATP PRODUCED DURING THE COMPLETE OXIDATION OF ACETOACETATE IN THE BRAIN IS

1) 2

2) 12

3) 23

4) 130

5) 36

257.SYNTHESIS OF FATTY ACIDS STARTS BY USING

1) glycerin

2) oxaloacetate

3) acetyl-CoA


5) malonyl-CoA

258.IN FATTY TISSUES AND MUSCLES DURING THE SYNTHESIS OF TRIACYLGLYCERIDES GLYCEROL-3 PHOSPHATE IS FORMED FROM

1) glycerol

2) acetyl-CoA

3) pyruvate


5) β-monoglyceride

259.LIPOTROPIC SUBSTANCES INCLUDE

1) high fatty acids

2) methionine

3) choline

4) triglycerides

5) vitamin B15, B12, B6, B9

260.SYNTHESIS OF CHOLESTEROL HAS THE FOLLOWING MAIN STAGES

1) formation of the mevalonic acid

2) formation of the phosphatidic acid

3) formation of squalene

4) formation of glycerol-3-phosphate

5) formation of lanosterine

261.SUBSTANCES, WHICH PREVENT FATTY DYSTROPHY IN THE LIVER

1) methionine

2) choline

3) insulin

4) vitamin B1

5) vitamin K

262.DURING SYNTHESIS OF HIGH FATTY ACIDS THE FOLLOWING SUBSTANCES TAKES PARTS

1) FADH2

2) NADH2

3) NADPH2

4) malonyl-CoA

5) ACP (acyl carrier protein)

263. SOURCES OF NADPH2 FOR LIPIDS BIOSYNTHESIS ARE

1) reactions of glycolysis

2) reactions of β-oxidation

3) reaction of pentose-phosphate pathway of glucose oxidation

4) reactions of urea cycle

5) oxidation of ketone bodies

264. THE FOLLOWING PROCESSES WHICH ACTIVATED DURING LONG TERM STARVING ARE

1) lipolysis in fatty tissue

2) β-oxidation in the liver

3) pentose-phosphate pathway of glucose oxidation

4) synthesis of ketone bodies in the liver

5) oxidation of glucose in muscular tissue

265.DEVELOPMENT OF ATHEROSCLEROSIS IS STIMULATED BY

1) increase in the contents of HDL in the blood

2) increase in the contents of LDL in the blood

3) decrease in the contents of LDL in the blood

4) decrease in the contents of HDL in the blood

5) decreasing of LDL receptors

266.KETONEMIA IS CAUSED BY

1) deficiency of glucagon

2) deficiency of insulin

3) starvation

4) renal dysfunction

5) disorder in Krebs cycle

267.ESTER BONDS IN MOLECULES OF TRIACYGLYCERIDES ARE HYDROLYZED BY THE ACTION OF ENZYME

1) phospholipase


3) lipase

4) non-specified esterase

5) acetylcholine esterase

268.GLYCEROL, APPEARED AT THE SPLITTING OF TRIACYGLYCERIDES, INDEPENDENTLY ON A WAY OF FURTHER TRANSFORMATION, FIRST OF ALL

1) is oxidized

2) is phosphorylated

3) is reduced

4) is methylated

5) is acylated

269.HIGH FATTY ACIDS IN PROCESS OF THEIR CATABOLISM ARE DESTROYED MAINLY BY WAY OF

1) reduction

2) deamination

3) β-oxidation

4) hydrolysis

5) decarboxylation

270.IN THE BIOSYNTHESIS OF HIGH FATTY ACIDS CARBON DIOXIDE IS USED FOR

1) formation of oxaloacetate

2) transforming of malonyl-CoA into acetyl-CoA

3) synthesis of CH3CO-CoA from pyruvate

4) ATP-dependent synthesis of malonyl-CoA from acetyl-CoA

5) formation of carbamoylphosphate

271.NAME VITAMINS WHICH ARE LIPOPHILIC SUBSTANCES

1) vitamin PP

2) vitamin K

3) vitamin H

4) vitamin E

5) vitamin F

272.INTERMEDIATE PRODUCTS OF THE DESTRUCTION OF HIGH FATTY ACIDS ARE

1) α-glycerol phosphate

2) β-hydroxybutyrate

3) acetyl-CoA

4) β-hydroxybutyryl-CoA

5) acyl-CoA(n-2)

273.CHOOSE NAME OF MULTIENZYME, CATALYZING WHOLE CYCLE OF BIOSYNTHESIS OF HIGH FATTY ACIDS

1) acetyl-CoA carboxylase

2) high fatty acids hydratase

3) acyltransferase

4) transacylase

5) high fatty acids synthetase

274.CHOOSE MAIN REASONS OF DISORDERS OF FAT DIGESTION AND ABSORPTION

1) disturbances of the synthesis of pancreatic lipase

2) absence of trypsin secretion

3) damaged delivery of bile into intestine

4) obstruction of pancreatic juice flow into intestine

5) insufficient secretion of HCO3 -

275.CHOOSE CORRECT PROPOSITIONS ABOUT PROPERTIES AND FUNCTIONS OF BLOOD LIPOPROTEINS:

1) chylomicrons are synthesized in adipose tissue, transport triacyglycerides into the blood

2) HDL are formed from LDL in blood by the action of lipoproteinlipase

3) VLDL are precursors of LDL

4) HDL compete with VLDL to binding the receptors on the surface of cells

5) HDL transport cholesterol from peripheral tissues to liver

276.PHOSPHATIDYLCHOLINE IS

1) triacylglycerol

2) glycolipid

3) glycerophospholipid

4) terpene

5) steroid

277.FUNCTION OF BILE ACIDS ARE

1) decomposition of triacylglycerols

2) emulsification of lipids

3) absorption of glycerol

4) facilitation of cholesterol and fatty acids absorption

5) inactivation of pancreatic lipase

278.THE PLACE OF CHYLOMICRONS SYNTHESIS IS

1) adipose tissue

2) liver

3) intestine

4) kidney

5) blood plasma

279.THE PLACE OF LDL BIOSYNTHESIS IS

1) intestine

2) liver

3) adipose tissue

4) kidney

5) blood plasma

280.BIOLOGICAL ROLE OF CHYLOMICRONS IS

1) transport of exogenous lipids

2) transport of endogenous cholesterol to the liver

3) transport of endogenous lipids

4) transport of endogenous phospholipids to the tissue

5) transport of endogenous triacylglycerols to the tissue

281.THE MAIN BIOLOGICAL FUNCTION OF LDL IS


2) transport of cholesterol to the liver


4) transport of phospholipids to the tissue

5) transport of cholesterol to the tissue

282.THE MAIN BIOLOGICAL FUNCTION OF HDL IS


2) transport of cholesterol to the tissues


4) transport of cholesterol to the liver

5) transport of triacylglycerols to the tissue

283.NAME THE PROCESS HAVING METABOLITES IN THE ORDER: ACETYL-COA, ACETOACETYL-COA, HMG-COA (β-HYDROXYL- β-METHYLGLUTARYL-COA), ACETOACETATE

1) β-oxidation of fatty acids

2) biosynthesis of keton bodies

3) biosynthesis of triacylglycerols

4) biosynthesis of cholesterol

5) biosynthesis of phospholipids

284.NAME THE PROCESS HAVING METABOLITES IN THE ORDER: ACETYL-COA, ACETOACETYL-COA, HMG-COA (β-HYDROXYL-β-METHYLGLUTARYL-COA)

1) β-oxidation of fatty acids

2) biosynthesis of keton bodies

3) biosynthesis of triacylglycerols

4) biosynthesis of cholesterol

5) biosynthesis of phospholipids

285.60. BIOLOGICAL FUNCTION OF LIPOTROPIC FACTORS IS

1) increasing of cholesterol biosynthesis

2) inhibition of cholesterol biosynthesis

3) increasing of keton bodies biosynthesis

4) inhibition of keton bodies biosynthesis

5) increasing of glycerophospholipids biosynthesis

286.COMPONENTS OF LIPOPROTEINES ARE

1) protoporphyrin

2) apolypoprotein

3) lipid nucleus, formed by triglycerides and cholesterol ethers

4) external layer containing polar phospholipids, cholesterol and apolipoproteins

5) carbohydrates

287.IN THE STRUCTURE OF THE LIPID BILAYER OF CELLULAR MEMBRANES WE CAN FIND

1) cholesterol

2) phosphatidylinositols

3) phosphatidylholin

4) sphingolipids

5) phosphatidylethanolamines

288.MEMBRANE PARTICIPATES IN

1) transfer of information from signaling molecules

2) regulation of metabolism in cells

3) transport of atp from cytosol into mitochondrial matrix

4) regulation of the flowing of substances in the cell and out of the cell

5) intercellular contacts

289.THE COMPOSITION OF CELL MEMBRANES INCLUDES LIPIDS

1) phospholipids

2) cerebrosides

3) gangliosides

4) cholesterol


290.PHOSPHOLIPIDS OF CELL MEMBRANES

1) diphosphatidylglycerols (cardiolipids)

2) phosphatidylcholines

3) phosphatidylethanolamines

4) phosphatidylinositols


291.The bilayer of the membrane is formed by such lipids as

1) phospholipids

2) triglycerides

3) fatty acids

4) cholesterol

5) diglycerides

292.The main mechanism of damage of the structure of cell membranes is

1) lipid peroxidation


3) vitamin B6 deficiency

4) vitamin K deficiency

5) vitamin D deficiency

293.INCOMPLETE digestion OF FATS IN THE GASTROINTESTINAL TRACT is CONNECTED WITH enzyme DEFICIENCY

1) amylase

2) pepsin

3) enterokinase

4) lactases

5) pancreatic lipase

294.ANTIATEROGENIC PROPERTIES HAVE

1) chylomicrons

2) HDL

3) LDL

4) VLDLP

5) cholesterides

295.IN THE HUMAN ORGANISM, can NOT BE SYNTHESIZED

1) triglycerides

2) ketone bodies

3) cholesterol

4) polyunsaturated fatty acids

5) saturated fatty acids

296. TRIGLICERIDES CONTAINS ALCOHOL

1) glycerol

2) cholesterol

3) inositol

4) sphingosine

5) retinol

297.EMULsification OF FATS HAPPENS in

1) oral cavity

2) stomach

3) small intestine

4) the large intestine

5) gallbladder

298.choose substances which CAN be SYNTHESIZEd FROM CHOLESTERol

1) bile acids

2) vitamins of group D

3) sex hormones

4) corticosteroids


299.LOCALIZATION OF THE PROCESS OF HIGH FATTY ACIDS OXIDATION IN THE CELL

1) nucleus

2) cytoplasm

3) mitochondria

4) ribosomes

5) lysosomes

300.Transfer of fatty acid through the Mitochondria membrane realizes

1) albumin

2) malate

3) carnitine

4) citrate

5) anserine

301.LOCALIZATION OF THE PROCESS OF HIGH FATTY ACIDS SYNTHESIS IN THE CELL

1) nucleus

2) cytoplasm

3) mitochondria

4) ribosomes

5) lysosomes

302. LIPOLYSIS IN FATTY tissue IS inhibited by

1) adrenaline

2) glucagon

3) insulin

4) thyroxine

5) corticotropin

303. they ARE NOT LIPIDS

1) cholesterol

2) triglycerides

3) phosphoproteins

4) fatty acids

5) wax

304.COMPONENTS OF LIPOPROTEINS ARE

1) phospholipids

2) esters of cholesterol

3) triacylglycerols

4) cholesterol


305.LIPOPROTEINS OF BLOOD PLASMA have FUNCTION

1) energy source

2) regulatory

3) transport

4) plastic

5) protective

306.Atherogenic are

1) micelles

2) chylomicrons

3) LDL

4) HDL


V. V topic. Metabolism of proteins

307.THE BALANCE OF NITROGEN IS OBSERVED IN THE FOLLOWING PERIODS

1) during the pregnancy

2) in the adult healthy person

3) on aged people

4) at the excessive arrival of proteins with food

5) on childhood

308.PROTEOLYTIC ENZYMES ARE ACTIVATED BY

1) splitting off the part of a peptide

2) phosphorylation of proteins

3) releasing of the active centre

4) disintegration of proteins on subunits

5) all above listed is true

309.BIOLOGICAL VALUE OF FOOD PROTEINS IS DEFINED BY

1) quantity of proteins accepted with food

2) presence of irreplaceable amino acids

3) animal proteins

4) ability of proteins to be digested

5) ability to maintain nitrogenous balance

310.NEUTRALIZATION OF TOXIC PRODUCTS OF DECAY OF AMINO ACIDS OCCURS

1) in the intestines

2) in the blood

3) in the liver

4) in the pancreas

5) in the spleen

311.THE FOLLOWING WAYS OF DEAMINATION OF AMINO ACID ARE MOST TYPICAL FOR MAN

1) intramolecular

2) oxidative

3) hydrolytic

4) regenerative

5) transdeamination (indirect deamination)

312.PRODUCTS OF DECARBOXYLATION OF AMINO ACIDS IN TISSUES AND INTESTINES ARE

1) oxaloacetate

2) piruvate

3) 5-oxitriptamine

4) g-aminobutyric acid

5) cadaverine

313.THE PROCESS OF INDIRECT OXIDATIVE DEAMINATION INCLUDES

1) hydration of fumarate

2) carboxylation of pyruvate

3) oxidative deamination of glutamate

4) transamination with the participation of a-ketoglutarate

5) decarboxylation of amino acids

314.NITROGEN-FREE RESIDUE IS PARTICIPATES IN

1) the synthesis of the non-essential amino acids

2) oxidation up to СО2 and Н2О

3) synthesis of glucose

4) synthesis of ketone bodies

5) synthesis of the higher fatty acids

315. THYROSINE IS THE PRECURSOR OF SUCH BIOLOGICALLY ACTIVE SUBSTANCES AS

1) cortizone

2) noradrenaline

3) thyroxine

4) adrenaline

5) androsterone

316.THE REACTION OF TRANSAMINATION SERVES FOR SYNTHESIS OF

1) glutamin

2) non-essential amino acids

3) essential amino acids

4) hydroxylic acids

5) higher fat acids

317.GLYCOGENIC AMINO ACIDS ARE

1) alanine

2) leucine

3) serine

4) phenylalanine

5) aspartate

318.KETOGENIC AMINO ACIDS ARE

1) alanine

2) leucine

3) serine

4) phenylalanine

5) aspartate

1) 319.AMINO ACIDS WHICH THE ACCEPTORS OF AMMONIA AT THE MOMENT OF ITS FORMATION IN THE CNS CELLS ARE

2) аlanine

3) аspartate

4) glycine

5) glutamate

6) phenylalanine

320.CHOOSE ENZYMES PARTICIPATING IN THE METABOLISM OF AMINO ACIDS

1) decarboxylase

2) aminotransferase

3) glutamatedehydrogenase

4) hexokines

5) pyruvatecarboxylase

321.VARIANTS OF AMMONIA NEUTRALIZATION IS

1) formation of amides

2) formation of urea

3) regenerative amination

4) formation of ammonia salts

5) formation of the uric acid

322.THE SYNTHESIS OF UREA IS CATALYZED BY

1) arginase

2) ornithincarbamoyltransferase

3) argininosuccinate synthetase

4) acylcarnitinetransferase

5) carbamoylphosphatesynthetase

323.THE EXCRETION OF AMMONIUM SALTS FROM KIDNEYS IS NECESSARY FOR

1) discharge of acids

2) discharge of carbon

3) discharge of alkalis

4) preservation of ions of sodium in the organs

5) discharge of ions of sodium from the organs

324.CAUSES OF HYPERAMONEMIA IN THE ORGANISM CAN BE

1) congenital decreasing in the activity of enzymes of the оrnithinic cycle

2) disorder of formation and elimination of ammonium salts at nephrites

3) the increasing of gluconeogenesis processes from amino acids

4) the increasing of catabolism of amino acids

5) diseases of the liver

325.THE METABOLITE OF THE UREA PRODUCTION CYCLE IS

1) arginine

2) aspartic acids

3) lactate

4) carbamoylphosphate

5) ornithine

326.THE NEUTRALIZATION OF AMMONIA IS POSSIBLE IN THE PROCESSES OF

1) synthesis of biogenic аmines

2) synthesis of ammonium salts

3) formation of amides of dicarboxylic acids

4) synthesis of urea

5) reductive amination of ketoacids

327.АLCAPTONURIA DEVELOPS AS A RESULT OF THE DISORDER EXCHANGE OF

1) valine

2) arginine

3) tyrosine

4) tryptophan

5) alanine

328.DIRECT BILIRUBIN IS CHARACTERIZED BY THE FOLLOWING FEATURES

1) conjugated with the glucuronic acid

2) badly dissolves in water

3) on healthy people its quantity is higher than the amount of indirect bilirubin

4) easily enters the reaction with the ehrlich reagent

5) conjugated with the sulphuric acid

329.JAUNDICE OCCURS AT

1) the amount of direct bilirubin in the blood is higher than 30 mmole/l

2) atherosclerosis

3) affection of the liver parenchyma

4) occlusion of bile ducts

5) at increased hemolysis of erythrocytes

330.THE INCREASING OF THE AMOUNT OF NONCONJUGATED BILIRUBIN IN THE BLOOD IS CONNECTED WITH

1) the discharge of indirect deamination processes

2) increased hemolysis of erythrocytes

3) at the parenchymatous jaundice

4) disorder in the conjugation with the glucuronic acid in the liver

5) destruction of the great number of erythrocytes in newborns and immaturity of the mechanisms of bilirubin conjugation in the liver

331.AT ALKAPTONURIA IN URINE SUCH SUBSTANCE APPEARS AS

1) tyrosine

2) phenylalanine

3) the uric acid

4) homogentisic acid

5) indican

332.INDIRECT BILIRUBIN IS CHARACTERIZED BY THE FOLLOWING FEATURES

1) it is conjugated with glucuronic acid

2) badly dissolves in water

3) in the blood plasma it is connected with аlbumins

4) easily penetrates through the hematoencephalic barrier and damages the brain cells

5) conjugated with the sulphuric acid

333.NAME ENZYMES THAT ARE ENDOPEPTIDASES

1) trypsin

2) carboxypeptidaes

3) aminopeptidase

4) pepsin

5) chymotrypsin

334.POSITIVE NITROGEN BALANCE IS OBSERVED

1) in children growing

2) during pregnancy

3) during starvation

4) in healthy adult men with normal diet

5) during hard chronic disease

335.THE FEATURES OF PROTEIN EXCHANGE ARE:

1) in animals organism deposition of protein is impossible

2) the end products of protein are very toxic ammonia and urea

3) 8 amino acids is not synthesized in organism

4) proteins have specific and individual specificity

5) proteins must enter with foods permanently for nitrogen balance

336.ENZYMES WHICH PARTICIPATE IN THE DETOXIFICATION OF AMINO ACIDS PRODUCT OF PUTREFACTION ARE

1) arylsulfotransferase

2) carbamoylphosphate synthetase

3) glucuronosyltransferase

4) arginase

5) glutamate dehydrogenase

337.PATHOLOGICAL PRODUCT WHICH IS FORMED IN GASTRIC JUICE AT ACHLORHYDRIA (ABSENCE OF CHLORIC ACID) IS

1) lactate

2) blood

3) uric acid

4) keton bodies

5) urea

338.DETECT TOXIC PRODUCTS WHICH ARE FORMED IN THE PUTREFACTION FROM DIAMINOMONOCARBONIC ACIDS IN INTESTINE

1) indole

2) H2S

3) cadaverine

4) skatol

5) putrescine

339. DETECT OPTIMAL pH FOR PEPSIN ACTION

1) 6-8

2) 1,5-2,0

3) 4-6

4) 3,5-5,5

5) 2-4

340.CHLORIC ACID OF GASTRIC JUICE

1) denaturates proteins of food

2) produces optimal ph for pepsin

3) activates pepsin by allosteric way

4) promotes to iron absorption

5) leads to partial proteolysis of pepsin

341.THE TOXIC PRODUCTS WHICH FORMED IN THE PROCESS OF AMINO ACIDS PUTREFACTION IN LARGE INTESTINE ARE

1) indole

2) cadaverine

3) putrescine

4) urea

5) H2S

342.CHOOSE PATHOLOGICAL CHANGES WHICH IS OCCURRED IN GASTRIC JUICE

1) hyperchlorhydria

2) hypochlorhydria

3) achlorhydria (gastric anacidity)

4) achilia

5) porphyria

343.BIOLOGICAL ROLE OF PROTEIN DIGESTION IS

1) amino acid entry for protein biosynthesis in organism

2) the source of essential amino acids

3) formation of the product without special specificity

4) formation of easily absorbing products

5) amino acid entry for energy production

344.THE SUBSTANCES WHICH TAKE PART IN THE DETOXIFICATION OF TOXIC PRODUCT IN THE LIVER ARE

1) UDP-GA (UDP-glucuronic acid)

2) c-AMP

3) phosphoadenosyl phosphosulfate

4) NADP

5) ATP

345.NON-ESSENTIAL AMINO ACID GLYCINE IS NECESSARY FOR SYNTHESIS OF

1) heme

2) purine nucleotides

3) creatine

4) phospholipids

5) proteins

346.METHYL GROUP OF METHYONINE IS USED FOR BIOSYNTHESIS OF

1) carnitine

2) creatine

3) phosphatidyl choline from phosphatidyl ethanolamine

4) adrenalin from noradrenalin

5) urea

347.GLUTAMINE IS THE MAIN CARRIER AND THE DONOR OF NITROGEN. ITS NITROGEN IS USED FOR BIOSYNTHESIS OF

1) purine nucleotides

2) pyrimidine nucleotides

3) amino sugars

4) adrenalin

5) creatine

348. TRANSAMINATION HAS CHARACTERISTICS

1) it is the final stage of nonessential amino acids biosynthesis from a-ketoacids

2) the total number of amino acids is not changed during transamination in the cell

3) transamination is reversible process

4) NAD is coenzyme of aminotransferase

5) ammonia is not produced during transamination

349.FORMATION OF GLUTAMINE IS MORE INTENSIVE IN

1) brain tissues

2) kidney

3) skeletal muscle

4) myocardium

5) liver

350.DECARBOXYLATION OF HISTIDINE LEADS TO FORMATION OF

1) histones

2) histamine

3) glycine

4) glutamine

5) glutamate

351.THE MORE SPREAD AMINO ACIDS FOR REACTION OF TRANSAMINATION ARE

1) alanine

2) valine

3) aspartate

4) glutamate

5) arginine

352.THE STARTING COMPOUNDS FOR HEME BIOSYNTHESIS ARE

1) glycine and γ-amino butyric acid (GABA)

2) glycine and succinate

3) histidine and succinate

4) glycine and succinyl-CoA

5) histidine and succinyl-CoA

353.NON-PROTEIN NITROGEN COMPOUNDS ARE

1) nitrogen of all nitrogen containing substances of blood

2) nitrogen of all proteins of blood

3) nitrogen of urine proteins

4) nonprotein nitrogen of urine

5) all nonprotein nitrogen containing molecules of blood

354.CHOOSE THE COMMON METABOLITE FOR BIOSYNTHESIS OF UREA AND KREBS CYCLE

1) succinate

2) aspartate

3) malate

4) fumarate

5) citrate

355.ACIDITY OF GASTRIC JUICE CONTAINS

1) total acidity

2) linked HCl

3) total HCl

4) free HCl

5) lactic acid

356.SOURCES OF PENTOSE FOR NUCLEIC ACIDS BIOSYNTHESIS ARE METABOLITES FROM

1) biosynthesis of glycogen


3) glycogenolysis

4) gluconeogenesis

5) glycolysis

357.HYPERURICEMIA (THE INCREASE OF URIC ACIDS’ AMOUNT IN BLOOD PLASMA) IS OBSERVED AT

1) the increase of purine synthesis rate

2) the decrease of purine excretion rate

3) the increase of purine catabolism at such diseases as cancer, leukemia

4) the decrease of the reaction of reutilization

5) the decrease of blood ph as a result of the decrease of filtration uric acid

6) in the kidney

358.GOUT (PODAGRA) IS CHARACTERIZED BY INCREASING OF CONCENTRATION OF

1) urea

2) creatinine

3) uric acid

4) creatine

5) bilirubin

359.FORMATION OF PURINES RING (PURINES BIOSYNTHESIS DE NOVO) OCCURS WITH THE HELP OF

1) amino acids (aspartate, glutamate, glycine)

2) CO2

3) methenyl-H4-folate (met-THFA)

4) glutamine

5) carbamoyl phosphate

360.SOURCES OF NITROGENIC ATOMS IN THE PURINE RING

1) urea

2) aspartic acid

3) glutamine

4) tryptophan

5) glycine

361.THE SYNTHESIS OF PYRIMIDINE NUCLEOTIDES IS CARRIED OUT WITH THE PARTICIPATION OF

1) 5-phosphoribozil-1- pyrophosphate

2) glycine

3) CO2, glutamine, ATP

4) carbamoylphosphate

5) tetrahydrofolic acid

362.A (PODAGRA) GOUT IS CHARACTERIZED BY

1) discharge in the exchange of purine nucleotides

2) discharge in the exchange of pyrimidine nucleotides

3) hyperuremia

4) the diet rich in meat products can promote it

5) deformation of joints, formation of renal calculi

363.DISINTEGRATION OF PYRIMIDINE NUCLEOTIDES IS ACCOMPANIED BY THE FORMATION OF

1) ammonia, СО2, Н2О

2) ammonia, Н2О2

3) β-alanine

4) hypoxanthine

5) the uric acid

364.CHOOSE FROM THE LISTED CONDITIONS THE POSSIBLE CAUSES OF GOUT

1) excessive synthesis of purine nucleotides

2) excessive intake of nucleic acids with food

3) decrease in the rate of reutilization of pyruvate bases

4) decrease in the rate of the uric acid formation

5) accumulation of the homogentisinic acid

365.REACTIONS WHICH BLOCKED BY THE ANTIVITAMINS OF THE FOLIC ACID ARE

1) biosynthesis of IМP

2) transformation of serine into glycine

3) biosynthesis of DNA

4) biosynthesis of polysaccharide

5) synthesis of АMP from IМP

366.ORNITHINe CYCLE OF UREA PRODUCTION TAKES PLACE

1) in the bladder

2) in the pancreas

3) in the intestines

4) in the liver

5) in the adrenal glands

367.AMMONIA IS NOT DECOMPOSED BY

1) amides formation

2) formation of urea

3) formation of uric acid

4) reductive amination

5) formation of ammonium salts

368.GOUT IS NOT CHARACTERIZED BY

1) disorders in the exchange of purine nucleotides

2) disorders in the exchange of pyrimidine nucleotides

3) hyperuricemia

4) a diet rich in meat products

5) joint deformity, kidney stones

369.α-DECARBOXYLATION OF AMINO ACIDS leads to FORMation of

1) СО2 and kinin

2) СО2 and amino acids

3) СО2 and keto acids

4) СО2 and hydroxy acids

5) СО2 and biogenic amines

370.ENZYME SPLITTING PROTEINS

1) amylase

2) pepsin

3) urease

4) catalase


371.PURINE NUCLEus CONTAINS

1) adenine

2) cytosine

3) uracil

4) thymine

5) thiamine

372.ORNIThINe CYCLE IS

1) formation of uric acid

2) urea biosynthesis

3) glucose oxidation

4) Corey cycle

5) formation of glucose

373.PORPHIRIA IS THE RESULT OF THE disoder of

1) synthesis of urea

2) breakdown of purine nucleotides

3) decay of pyrimidine nucleotides

4) heme synthesis

5) hemoglobin degradation

374.ANEMIA IS THE result of

1) disorder of heme synthesis

2) iron deficiency in food

3) vitamin B12 deficiency

4) disorder of transport and deposition of iron


375.Pepsin is formed in

1) liver

2) small intestine

3) stomach

4) gall bladder

5) large intestine

VI. VI topic. Special biochemistry of organs and tissues

376.HORMONES HAVE THE FOLLOWING FEATURES

1) action of hormones is realized through protein receptors and intracellular intermediators

2) hormones act at very small amounts

3) hormones act by increasing the rate of enzymes synthesis de novo or changing their activity

4) hormones are not substances of the organic nature

5) endocrine glands and produced by them hormones make the system of direct and reverse connection

377.HORMONES HAVING STEROID NATURE ARE

1) estradiol

2) glucagon

3) thyroxin

4) cortisol

5) testosterone

378.CHOOSE ENDOCRINE GLANDS WHICH PRODUCE PEPTIDE HORMONES

1) parathyroid gland

2) pancreas

3) testicles

4) hypophysis

5) ovaries

379.ACCORDING TO THE CHEMICAL NATURE HYPOTHALAMUS HORMONES ARE

1) complex proteins

2) derivatives of tyrosine

3) steroids

4) low-molecular peptides

5) derivatives of the arachidonic acid

380.ON THE OUTER SURFACE OF TARGET CELLS THE RECEPTORS FOR THE FOLLOWING HORMONES ARE LOCATED

1) glucagon

2) adrenalin

3) aldosterone

4) cortisol

5) testosterone

381.IN THE CYTOSOL OF TARGET CELLS THE RECEPTORS OF THE FOLLOWING HORMONES ARE LOCATED

1) Insulin

2) Adrenalin

3) Testosterone

4) Cortisol

5) Thyroxin

382.CALL THE SECONDARY MESSENGERS

1) АDP

2) c-АМP

3) c-GМP

4) АМP

5) Ca2+

383.CHOOSE THE PECULIARITIES OF LIBERINS AND STATINS FEATURES

1) they do not enter the systemic blood circulation

2) by the portal system they reach hypophysis

3) they act as stimulating or depressing agents on biosynthesis and secretion of hypophysis hormones

4) they are synthesized in hypothalamus

5) they are synthesized from carbohydrates

384.THE ANTERIOR LOBE HYPOPHYSIS HORMONES INCLUDE

1) adr

ii · web viewcreatine kinase, aldolase gpt, cholinesterase aldolase, lipase ldh1, got, ck 82. the...

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