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CLINICAL CHEMISTRY

CHAPTER 10

ENZYMES

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Introduction

Enzymes are the chemical lubricants that make chemical reactions go nice

and easy

They help out with chemical reactions -but they dont get used up

themselves ( sort of like the oil in your car hopefully )

They are always proteins ! ( Remember proteins ? )

Theyre found in cells throughout the body. When these cells get sick the

enzymes in them tend to ooze out into the plasma

Want to diagnose heart attacks, liver disease, muscle disease, pancreatitis,

prostate cancer and bone disease? Enzymes can do that !

They are different because we measure them not in terms of how many

there are ( mg / dl , for example ) but in terms of their activity ( how well they

are lubricating chemical reactions

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KEY TERMS

Activation energy

Activators

Apoenzyme

Catalyst

Coenzyme

Cofactor

Enzyme

First Order Kinetics

Second Order Kinetics

Isoenzymes

Holoenzyme International Unit (IU) of Enzyme

Activity

Kinetic Assay

2 - Point Assay

Substrate

Substrate Depletion

Zymogen

Prosthetic Group

Inhibitors

Competitive Inhibitors

Non - Competitive Inhibitors

Uncompetitive Inhibitors

Allosteric Site

Active Site

Michaelis - Menten Constant Myocardial Infarction ( MI )

Congestive Heart Failure ( CHF )

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The Enzymes we will study

CPK

ALK AST

ALT

GGT

LDH

AMY

LIP

ACP

SChE

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OBJECTIVES

Discuss the general structure and functions of enzymes

Define a unit of enzyme activity ( IU )

Discuss how temperature, pH and other factors effect enzyme activity

Explain first - order and zero - order enzyme kinetics and the special

techniques that are used to measure enzymes

Discuss the tissue sources, clinical significance and Normal Values of

the following

CPK, LDH, AST, ALT

ALK, GGT AMYL, LIP

ACID PHOS, Cholinesterase

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General Properties and Definitions

Many chemical reactions cannot occur at 37 ( too cold ) Many chemical reactions require added heat energy

Biochemical reactions also require this energy , but proteins will

denature

So how do biochemical reactions ever happen ? They cheat !!!

Biochemical reactions can occur if there is a way to lower the

amount of energy it takes to make the reaction happen.

So how do biochemical reactions cheat ???

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Answer : They get a catalyst

Catalysts are substances that lessen the amount of energy required forchemical reactions to occur

Catalysts are not used up in the reaction

Substrate Product

Enzymes are protein catalysts

Enzymes are required for the numerous metabolic processes of all cells

When cells are damaged, enzymes leak out into the plasma

The measurement of these enzymes are useful diagnostic tools

Enzyme

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Activation Energy for Chemical Reactions

Catalysts decrease the amount of energy required to activate chemical

reactions. Enzymes are protein catalysts.

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Enzyme Structure

Similar to protein structure, because all enzymes are proteins

1 Amino acid sequence

2 Interaction between 2 locations on the protein chain

3 Folding of chains ( 3D structure )

4 2 or more separate polypeptide chains

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Definitions

Active site

Physical location on the enzyme molecule which interacts with

the substrate molecule

Allosteric Site

Nonactive site , but which may interact with other

substances to change the overall enzyme 3D shappe

Isoenzymes

Structurally different enzymes ( proteins ) but which catalyze

the same chemical reactions

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Cofactor

A nonprotein substance required for normal enzyme activity Cofactors maintain enzyme 3D structure ( critical for enzyme

function )

There are 2 types of cofactors

Activators ( Inorganic --- Magnesium , Calcium )

Coenzyme ( Organic - NADH )

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Holoenzyme

Enzyme + coenzyme ( prosthetic group ) = Active enzyme

Proenzyme ( Zymogen , Apoenzyme )

Enzymecoenzyme = Inactive enzyme

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Enzyme Structure and Substrate

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Classification and nomenclature

Enzyme kinetics

Chemical reactions occur spontaneously if the energy for

reactants is higher than products

The amount of energy required to stimulate molecules to breaktheir chemical bonds and form new bonds is the activation

energy

Increasing the temperature can generate the activation energy.

This a problem for living cells

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Enzymes lower the activation energy for chemical reactions

The enzymesubstrate complex has a lower activation energythan the substrate alone

Enzymes are usually specific as to which chemical reactions they

catalyze

E + S ES E + P

Enzyme +

Substrate

EnzymeSubstrate

ComplexEnzyme + Product

The enzyme is not consumed or depleted by the chemical reaction

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Enzymes differ in their ability to react with different substrates

There are various enzyme specificities

Absolute : Catalyzes only 1 specific substrate

Group : Catalyzes reactions of a particular chemical group

Bond : Catalyzes reactions of particular chemical bonds

Stereoisomerism : Catalyzes reactions of steroisomers

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Factors that influence enzymatic factors

First Order Kinetics

Enzyme concentration exceeds substrate concentration

As substrate concentration increases , the reaction rate

increases

The reaction rate is proportional to substrate concentration

This is not a good place to measure enzyme activity

( The reaction rate is dependent on substrate , not enzyme )

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Zero Order Kinetics

Substrate concentration is in excess Substrate saturates enzyme

All enzyme reacts with the excess substrate

The chemical reaction rate goes to maximum velocity

Reaction rate is dependent on enzyme activity ( conc . )

Enzymes are not measured in terms of concentration , but

activity

Zero Order conditions are suited for enzyme measurementbecause this is where the reaction rate is dependent on the

enzymes ability to catalyze a chemical reaction

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Relationship between substrate concentration and

the reaction rate in a enzymatic reaction

Substrate concentration

Reaction

Rate

Zero Order conditions

First Order Conditions

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Enzyme concentration

Enzymes are not measured in terms of concentration

Enzymes are measured is terms of their activity

Enzyme activity = The rate at which an enzyme catalyzes a

chemical reaction

Increased activity is proportional to increased concentration

Activity is measured under Zero Order conditions because this is

where the reaction rate is dependent on the work ( activity ) of the

enzyme

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MICHAELIS-MENTEN CONSTANT (Km)

Numerical constant for each enzyme and substrate under definedconditions

Expresses a relationship between the reaction rate and substrate

concentration

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pH ( acidity )

Enzymes are proteins and subject to changes in 3D structure frompH changes

pH must be carefully controlled in enzymatic reactions

Temperature

Reactions rates vary dramatically with temperature changes

Reactions rates may double per 10 C increase in temperature

Temperature must be defined and regulated for enzymatic reactions

37 C is the common standardized temperature

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Cofactors ( non-protein substances needed for enzymatic activity )

Activators (Ca+2

, Fe+2

, Mg+2

, Mn+2

, Zn+2 )

Coenzymes ( Vitamins and nucleotide phosphates )

Increased coenzyme concentration increases reaction rate

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Inhibitors ( Substances that decrease enzyme reaction rates )

Competitive Inhibitors

Substances that bind at the enzymes active site

Competes with substrate for the active site

Addition of additional substrate increases the reaction rate

NonCompetitive Inhibitors

Substances that bind at an enzymes non active site

Enzymes 3D shape is altered, decreasing enzyme activity

Addition of additional substrate has no effect on reaction rate

Uncompetitive Inhibitors

Substances that bind with enzymesubstrate complex

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Effects of inhibitors on Km

Competitive Inhibitors increase Km

Non-competitive Inhibitors have no effect on Km( maximum velocity is not possible )

Un-competitive Inhibitors decrease Km

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Measuring enzyme activity

Enzymes are not directly measured

Enzymes are commonly measured in terms of their catalytic activity

We dont measure the molecule

We measure how much work it performs Its catalytic activity

The rate at which it catalyzes the conversion of substrate to product

The enzymatic activity is a reflection of its concentration

Activity is proportional to concentration

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Photometric measurement of activity

E + S ES E + P

Enzyme activity can be tested by measuring

Increase of product

Decrease of substrate

Decrease of co-enzyme

Increase of altered co-enzyme

If substrate and co-enzyme are in excess concentration, the

reaction rate is controlled by the enzyme activity.

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Coupled enzyme reactions

Some enzyme testing utilizes other enzymatic reactions in a

sequence of reactions.

These other accessory enzymes are not being measured.

Auxillary enzymes are used as reagents and added in excess so they donot become rate limiting factors in the overall process.

All enzymatic reactions in a coupled assay must be performed at zero

order kinetics.

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Example of a coupled assay

S1 + E1 S1 E1 E1 + P1 ( RXN 1)

P1 + E2 P1 E2 E2 + P2 ( RXN 2 )

P2 + E3 P2 E3 E3 + P3 ( RXN 3)

E1 = Enzyme we want to measure ( patient ) E2 = Auxiliary enzyme ( reagent )

E3 = Indicator enzyme ( reagent )

There are 3 reactions with 3 different enzymes

P1 becomes the substrate for reaction rxn 2

P2 becomes the substrate for reaction rxn 3

We end up measuring reaction 3, but its reaction rate is

determined by reaction rate of rxn 1

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Enzymatic reactions are measured in terms of the rate at whichsubstrate is converted into product. This can be done in 2 differentways.

FixedTime Assay ( 2 Point )

Zero Order Kinetics

Substrate concentration is measured at set timed intervals todetermine enzyme activity

A slight delay from the beginning of the reaction to maximumvelocity is the lag phase

These times intervals may not be short enough to detect suddenchanges

Extreme elevations in enzyme activity may deplete the substratebetween measured intervals - Substrate Depletion

Substrate depletion causes falsely decreased activity results.

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Two Point Enzyme Methodology

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Multipoint Continuous Monitoring ( Kinetic Assay )

Continuous measurements of substrateproduct concentrationare recorded by the spectrophotometer of an automated

analyzer

Substrate depletion is detected because the analyzer is always

looking and will see any sudden dramatic changes

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Multipoint Enzyme Method

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Comparison of 2 Point and Multipoint Enzyme Techniques

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Enzyme Activity can be measured as a function of the change of absorbance

values over a period of time

Remember that enzymes are measured in terms of activity

How much work is getting done? How fast are chemical reactions taking place?

A large change in absorbance per unit of time indicates that the reaction was

occurring at a rapid rate, meaning that enzyme activity is high

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Calculation of enzyme activity

Remember, its not concentration its activity

Enzymes are measured in terms of how fast they convert substrate into

product Activity is a measurement of how fast they work

The common unit of enzyme activity is the International Unit ( IU )

1 IU = That amount of enzyme that will convert 1micromole (1 mole ) of substrate to product per minuteunder defined conditions

These conditions are such things as

pH

Temperature

Substrate

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Mathematical expression of enzyme activity

A = The rate of change in Absorbance ( A ) of the

substance being measured

MIN = Time the reaction is measured

TV = Total sample volume ( patient plasma + reagents )

SV = Volume of patient plasma

106 = Conversion of moles into micromoles

L = Length of the light path = Molar absorptivity

610LX1(IU/L)ACTIVITYENZYME

SV

TV

MIN

A

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Example of Molar Absorptivity calculation

NADH ( a common co-enzyme ) absorbs light at 340 NM

NAD ( the reduced form ) does not absorb light at 340 nm

Increased ( or decreased ) NADH concentration in a solution will

cause the Absorbance ( A ) to change.

A 0.05 X 10-3 Molar NADH solution placed in a 1 cm lightpath has an absorbance of 0.311

LMOLES/10X6.221CMXRMOLES/LITE10X0.05

0.311

3

3-

The molar absorptivity of NADH is 6.22 x 103 Moles / Liter

Each chemical substance has its own unique molar absorptivity

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Enzymes as reagents

Enzymes are used as reagents in a wide variety of methodologies

to measure other non-enzyme substances

Enzymes help to produce substances that can be easily measured

Enzyme specificity helps to eliminate interfering substances

If the enzyme is used as a reagent, we do not want the enzyme

concentration to be a affect the chemical reaction To avoid this the enzyme is added in excess so that it cannot

become a rate limiting factor .

Remember, we are just using the enzyme to measure something

else

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Creatine Kinase ( CK , CPK )

CPK catalyzes

Creatine + ATP Creatine phosphate + ADP

High concentrations of CPK in muscle, cardiac and brain tissues

Increased plasma CPK activity is associated with damage to thesetissues

CPK is especially useful to diagnose

AMIs Skeletal muscle diseases ( Muscular Dystrophy )

CPK

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CPK ( cont )

CPK has 3 isoenzymes

Each isoenzyme is composed of two different parts ( dimers )

CK - BB BRAIN

CK - MB CARDIAC

CK - MM SKELETAL MUSCLE

Skeletal muscle CPK is 99% CK-MM

Cardiac muscle CPK is 80% CK-MM and 20% CK-MB

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CPK ( cont )

Most normal plasma CPK is CK-MM

Because of CKMBs association with cardiac tissue,

increased CPKMB ( > 6% of the total CPK activity ) is a

strong indication of AMI

Post AMI CPK - MB

CK-MB increases 48 hours post AMI

Peaks at 12 - 24 hours post AMI

Returns to normal 24 - 48 hours later

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CPK ( cont )

CPK assays are often coupled assays CPK

In the example below, the rate at which NADPH is produced is a

function of CPK activity in the first reaction.

Hexokinase and G6PD are auxiliary enzymes

Creatine Phosphate + ADP Creatine + ATP

ATP + Glucose Glucose 6 - Phosphate

G6 - P + NADP 6 - Phosphogluconate + NADPH

CPK

Hexokinase

G6PD

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CPK ( cont )

RBCs lack CPK, but hemolyzed RBCs release adenylate kinase into

the plasma, causing falsely increased CPK activity

Hemolyzed specimens must be recollected

Reference ranges

Males Total CPK 15 - 160 IU / L

Females Total CPK 15 - 130 IU / L

Lets remember 15 150 IU / L

CK - MB: < 6 % of Total CPK

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Lactate dehydrogenase ( LDH , LD )

LDH is found in many different tissues

Skeletal muscle

Cardiac muscle

Renal tissue

RBCs

Plasma LDH activity is elevated in a variety of conditions

Liver disease

Cancers

AMI

Hemolytic diseases

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LDH ( cont )

LDH post AMI

Increases 1224 hours post AMI

Peaks at 4872 hours

May remain elevated for 10 days

RBC hemolysis falsely increases plasma LDH

Reference range : 100 - 225 IU / L ( L P )

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LDH Isoenzymes

Because increased total LDH is relatively non-specific, LDH

isoenzymes can be useful

5 isoenzymes composed of a cardiac ( H ) and muscle ( M )

component

LD - 1 ( HHHH ) Cardiac , RBCs LD - 2 ( HHHM )

LD - 3 ( HHMM ) Lung, spleen, pancreas

LD - 4 ( HMMM ) Hepatic and skeletal

LD - 5 ( MMMM )

A flipped LD - 1 / LD - 2 ( LD-1 > LD-2 ) consistent with

AMI

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Aspartate Aminotransferase ( AST, SGOT, GOT )

High concentrations of AST are found in

Skeletal muscle

Cardiac muscle

Liver tissue

Lung tissue

Post AMI

Rises 68 hours

Peaks at 24 hours

Returns to normal by day 5

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AST ( cont )

AST assays usually utilize a coupled enzyme technique

Aspartate + - Keto - Glutarate Oxaloacetate + Glutamate

Oxaloacetate + NADH + H Malate + NAD

MD is an auxiliary enzyme

NADH absorbs light at 340 nm NAD does not

Reference Range : 5 - 30 IU / L

AST

MD

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Chemical reactions of the amino-transferases AST and ALT

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Alkaline phosphatase ( ALK, ALK PHOS )

Optimal pH at 9.010.0 ( alkaline )

Removes phosphates ( PO4 ) from organic compounds Requires Mg as an activator

High concentrations in

Bone Liver

Best utilized to diagnose bone and liver disease

Reference range : 3090 IU / L

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Amylase ( AMY, AMYL )

Catalyzes breakdown of starch and glycogen to glucose

High concentrations in

Pancreas

Saliva Chew on some bread !!!

Amylase is filtered into the urine ( unusual for a protein )

Urine amylases are occasionally ordered

Increased plasma or urine amylase is very suggestive of

pancreatitis or pancreatic malignancy

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Amylase ( cont )

Because amylase is concentrated and excreted in the urine, urine

amylase values may be more diagnostic that plasma

Many different amylase methodologies varying in the types of

substrates used

Reference range : 60180 SU / dl

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Acid phosphatase ( ACP, Acid Phos )

Same function as ALK PHOS, but at a different pH

Optimal pH is 5.0 ( acid )

High concentrations in the prostate gland made it a useful test for

the diagnosis of prostate cancer

Its use is declining because of other, better tests for prostate cancer( Prostate Specific Antigen - PSA )

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GammaGlutamyltransferase ( GGT )

High concentrations in liver tissue

Increased plasma GGT is associated with

Hepatobiliary disease

Alcoholic cirrhosis

Insurance companies utilize GGT to detect alcoholism

Reference range : 645 IU / L

GGT

Glutathione + amino acid Glutamylpeptide + L-Cysteine

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Lipase ( LIP )

Hydrolyze ( breaks down ) fat

High concentrations in the pancreas .

Increased plasma lipase associated with pancreatitis

Lipase is more specific than amylase for the detection of

pancreatitis

Reference range : 0.0 - 1.0 U / ml

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Pseudocholinesterase ( SChE )

Considered a screening test for exposure to organophosphate exposure

( pesticides)

SChE is found in plasma, liver, pancreas and brain

Reference Range : 4,000 - 12000 IU / L

( )

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Diagnosis of AMI ( Acute Myocardial Infarction )

Remember cardiac disease is the #1 cause of death in the United States

#1 Symptoms, physical examination , and patient history But there are many causes of chest pain other than AMI

#2 EKG only 50% reliable - may be normal even during AMI

#3 Laboratory tests ( Troponin I , CKMB , Myoglobin , BNP )

Cardiac cellular necrosis following ischemic event causes soluble proteins

to leak into the plasma

Rephrased : When coronary arteries are blocked ( ischemic event ) cardiac

tissue is deprived of oxygen and dies, and dead cardiac tissue cells spilltheir guts into the plasma

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Myoglobin

Soluble heme protein

Present in all muscle cells, cardiac and skeletal Plasma myoglobin is elevated in various forms of muscle damage -

surgery, strenuous exercise, degenerative muscle diseases and physical

trauma

Myoglobin can also be elevated from decreased renal clearance

Relatively low molecular weight , water solubility and high cellular

cytoplasm concentrations cause myoglobin to be the first marker to be

released from damaged cells

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Troponin I

Contractile protein associated with cardiac and skeletal tissue

Two forms Troponin I and Troponin T

Troponin I from cardiac tissue has a unique antigenic structure that

differentiates it from skeletal Troponin I and facilitates its measurement

Of all the cardiac markers , Troponin I is the most specific for cardiac

injury

CK-MB

Iso-enzyme found in cardiac and skeletal tissue

Plasma CKMB concentrations are increased in AMI and various forms of

skeletal muscle trauma Although not absolutely specific, very high concentrations in cardiac

tissue make it a good marker for AMI

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B- Type Natremic Protein ( BNP )

Increased plasma BNP is associated with Congestive Heart Failure ( CHF )

CHF is one of the most common reasons for hospitalization in patients greater

than 70 years old

BNP assays are often ordered with AMI markers to differentiate between AMIs

and CHF

BNP in normal in AMI

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Cardiac enzymes

In the good old days , AMIs were diagnosed with the cardiac

enzymes

The cardiac enzymes consisted of Total CPK, LDH and AST

Although still useful, the more specific markers such as

Troponin I, Myoglobin and CK-MB have largely replaced the

cardiac enzymes

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TRIAGE CARDIAC PANEL FOR RAPID QUANTIFICATION OF

CK-MB, MYOGLOBIN , TROPONIN I and BNP

TRIAGE is a common commercial test package that quantitates the

three most significant laboratory markers for AMI - CK-MB ,

Troponin I and Myoglobin

Procedure summary Lithium heparin whole blood is added to the cartridge system

Plasma separates from RBCS after passing through a filter

Plasma ( CK-MB , Troponin I and Myoglobin ) reacts with fluorescent

tagged anti-CKMB, anti-Troponin and anti-Myoglobin monoclonal

antibodies in the reaction chamber Concentration of the analyte is directly proportional to fluorescence that

is measured on the Triage Meter

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Summary of Triage cardiac markers after AMI

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Summary of Triage cardiac markers after AMI

Increases Peaks Normal

Myoglobin 2 hrs 6 8 hrs 20 36 hrs

Troponin I 4 8 hrs 12 16 hrs 6 10 days

CK MB 4 8 hrs 12 24 hrs 72 hrs

Although any single analyte may not be adequate to diagnose an AMI, the

collective information from all three analytes can be very useful

The interpretation of cardiac markers can be difficult because blood specimens

are not always collected soon after patients suffer chest pains - delays of hours

to days are common before patients seek medical attention

The most common symptom of a heart attack is .

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Enzyme Top 10

Enzymes are protein catalysts that lower activation energy of chemical reactions

Enzymes are not consumed in the reactions they catalyze

Enzymes are measured in terms of activity ( know the definition of an IU )

Enzymes are measured at zero order kinetics

CPK Cardiac and skeletal muscle

ALK Bone and hepatic tissue

GGT and ALP Hepatic tissue

AMY and LIP Pancreas

LDH Hepatic, Cardiac , RBCs ( lots of others ) AST Cardiac, Hepatic and skeletal

CK-MB Cardiac ( good to diagnose AMI )

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REFERENCE RANGES

ALT 5 - 35 IU/L

AST 5 - 30 IU/L CPK 15 - 150 IU/L

GGT 5 - 45 IU/L

LDH 100 - 225 IU/L

ALK 30 - 90 IU/L

AMYL 60 - 180 SU/Dl

LIPASE 0.0 - 1.0 IU/ML

CK-MB LESS THAN 6% OF CPK

ACID PHOS 3.0 - 12.0 IU/L

MYOGLOBIN 3090 mg/dl TROPONIN I < 0.6 ng/ml

BNP < 100 pg/ml

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Enzyme Links

http://www.bact.wisc.edu/microtextbook/Metabolism/Enzymes.html

http://med6.bham.ac.uk/teaching/clinyear3/enzymslide/

http://ull.chemistry.uakron.edu/genobc/Chapter_20/

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Enzymes.html

http://www.bact.wisc.edu/microtextbook/Metabolism/Enzymes.htmlhttp://med6.bham.ac.uk/teaching/clinyear3/enzymslide/http://med6.bham.ac.uk/teaching/clinyear3/enzymslide/http://www.bact.wisc.edu/microtextbook/Metabolism/Enzymes.html