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Clinical Chemistry > ENZYMES > Flashcards

ENZYMES Flashcards

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1
Q

Higher the enzyme concentration, the faster is the reaction, because more enzyme is present to bind with substrate

A

Enzyme Concentration

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2
Q

The reaction rate steadily increases as more subtrate is added

A

Substrate concentration

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3
Q

Organic Compound
Increasing its concentration will increase the velocity of an enzymatic reaction
Essential to achieve absolute enzymatic activity
Ex: NAD & NADH

A

Coenzymes

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4
Q

Inorganic ions which alters the spatial configuration of enzyme for proper substrate binding
Ex: Calcium, Zinc, Chloride, Magnesium & Potassium

A

Activators

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5
Q

Inorganic ion attached to a molecule
Ex: Catalase & Cytochrome Oxidase

A

Metalloenzymes

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6
Q

Physically binds to the active site of an enzyme
Inhibition is reversible when the substrate concentration is significantly higher than concentration of inhibitor

A

Competitive Inhibitor

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7
Q

Does not compete with substrate but look for areas other than the active sire
Subtrate & Inhibitor may bind an enzyme simultaneously

A

Non-Competitive Inhibitor

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8
Q

Inhibitor binds to the enzyme-substrate (ES) complex
Increasing substrate concentration results to increase inhibition

A

Uncompetitive Inhibitor

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9
Q

Enzymes having the same catalytic reactions but slightly different molecular structures because of differences in the amino acid sequence of enzymes

A

Isoenzymes

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10
Q

Enzymes are active at what temperature?

A

25C
30C
37C (Optimum)

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11
Q

Most physiologic reactions occur in the pH range of ___

A

7 to 8

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12
Q

Ideal temperature for preservation of enzymes

A

-20C

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13
Q

Ideal storage temperature for substrates and coenzymes

A

2 - 8C

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14
Q

Ideal for storage of LDH
LDH4
LDH5

Cold labile LDH

A

22C or Room temperature

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15
Q

Catalyze the removal or addition of electrons
Ex:
1. CO
2. LDH
3. MDH
4. ICD
5. G-6-PD

A

Oxidoreductases

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16
Q

Catalyze the transfer of a chemical group other than hydrogen form one substrate to another
Ex:
1. CK
2. AST
3. ALT
4. OCT

A

Transferases

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17
Q

Catalyze hydrolysis or splitting of a bond by the addition of water
Ex:
1. ACP, ALP, CHS, LPS
2. Trypsin, Pepsin, LAP
3. AMS, Galactosidases

A

Hydrolases

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18
Q

Catalaze removal of groups from substrates without hydrolysis
Ex:
1. Glutamate decarboxylase
2. Pyruvate decarboxylase
3. Tryptophan decarboxylase
4. Aldolase

A

Lyases

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19
Q

Catalyze the intramolecular arrangement of the substrate-compound
Ex:
1. Glucose phosphate isomerase
2. Ribose phosphate isomerase

A

Isomerases

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20
Q

Catalyze the joining of two substrate molecules, coupled with breaking of pyrophosphate bond in ATP or similar compound
Ex:
1. Synthase

A

Ligases

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21
Q

Reaction rate depends only on enzyme concentration

A

Zero-order reaction

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22
Q

Reaction rate is directly proportional to substrate concentration

A

First-Order reaction

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23
Q

Hig Specificity Enzymes:

A

Acid Phosphatase
Alanine Aminotransferase
Amylase
Lipase

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24
Q

Principal tissues of High Specificity enzymes:

A
  1. ACP - RBC & Phosphate
  2. ALT - Liver
  3. Amylase - Pancreas, Salivary gland
  4. Lipase - Pancreas
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25
Q

Moderate Specificity Enzymes:

A
  1. Aspartate Aminotransferase
  2. Creatinine Kinase
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26
Q

Principal tissues of Moderate Specific Enzymes

A
  1. AST - Liver, Heart, Skeletal Muscles
  2. CK - Brain, Heart, Skeletal Muscles
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27
Q

Low Specificity Enzymes

A
  1. Alkaline Phosphate
  2. Lactate Dehydrogenase
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28
Q

Principal tissues of Low Specific Enzymes:

A
  1. ALP - Liver, Bone, Kidney
  2. LDH - All tissues
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29
Q

Nonspecific enzyme capable of reacting with many different substrates
Liberates inorganic phosphate from an organic phosphate ester with concominant production of an alcohol

A

Alkaline Phosphate

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30
Q

Major Isoenzymes of ALP

A
  1. Liver ALP
  2. Bone ALP
  3. Placental ALP
  4. Intestinal ALP
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31
Q

Reference Value of ALP:

A

30 - 90 U/L

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32
Q

ALP is higher in individuals of blood group ___ because of differences in intestinal ALP levels

A

Group B & O

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33
Q

Inc. ALP is the Major liver fraction that is most frequently elevated especially in what disease___

A

Obstructive Jaundice

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34
Q

For bone disorders, highest elevations of ALP occurs in what disease?

A

Paget’s Disease
Osteitis deformans

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35
Q

Found in lung, breast, ovarian and gynecological cancers
Bone ALP co-migrator
Most heast stable ALP (65C for 30 mins)
Inhibited by Phenylalanine reagent

Carcinoplacental ALP

A

Regan ALP

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36
Q

Found in adenocarcinoma of pancreas and bile duct, pleural cancer
Inhibited by L-leucine and phenylalanine

A

Nagao ALP

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37
Q

Most anodal isoenzyme:

A

Liver ALP
Bone ALP

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38
Q

Least Anodal ALP

A

Intestinal ALP

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39
Q

Performed at 56C for 10-15 minutes

A

Heat Fractionability/ Stability Test

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40
Q

Most heat Stable Isoenzyme:

A

Placental ALP

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41
Q

Most Heat Labile ALP

A

Bone ALP

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42
Q

Decreasing order of ALP heat stability

A

Placental, Intestinal, Liver, Bone

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43
Q

This method uses different concentrations of phenylalanine, synthetic urea and levamisole solutions

A

Chemical Inhibition Test

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44
Q

L-phenylalanine inhibits what isoenzyme of ALP?

A

Placental
Intestinal

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45
Q

3M Urea inhibits what isoenzyme of ALP

A

Bone ALP

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46
Q

Levimasole reagent inhibitis what ALP

A

Liver ALP
Bone ALP

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47
Q

Reference Method & Most Specific method in determining ALP levels:

A

Bowers & McComb
(Szasz Modification)

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48
Q

Substrate of the Bowers & McComb method:

A

p-nitrophenylphosphate

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49
Q

End product of Bowers & McComb Method:

A

p-nitrophenol or
Yellow nitrophenoxide ion

50
Q

What is a component ALP?
What is its enzyme activator?

A
  1. Zinc
  2. Magnesium
51
Q

Decreased ALP is seen in what deficiency:

A

Zinc deficiency

52
Q

Useful tumor marker in serum and CSF for most germ cell tumors

A

Placental Alkaline Phosphatase (PLAP)

53
Q
  1. Osteitis deformans
  2. Obstructive jaundice
  3. Osteomalacia
  4. Rickets
  5. Osteoblastic bone tumors
  6. Sprue
  7. Hyperparathyroidism
  8. Hepatitis and Cirrhosis
A

Increased ALP

54
Q

Catalyzes the same reaction made by ALP, except that it is active at pH 5.0
Levels >50 IU/L indicates presence of seminal fluid in the sampe:

A

Acid Phosphatase

55
Q

Tissue sources of ACP

A
  1. Prostate (Major source)
  2. RBCs
  3. Platelets
  4. Liver
  5. Bone
56
Q

Reference Value of ACP:

A

Male: 2.5-11.7 U/L (Total ACP)

57
Q

ACP is used for the detection of what cancer:

A

Prostatic Adenocarcinoma

58
Q

Seminal-fluid ACP activity can persists for up to how many days?

A

4 days

59
Q

What is the specific substrate used and the substrate of choice for quantitative endpoint reaction for ACP

A

Thymolphthalein monnophosphate

60
Q

Substrate preferred for continuous monitoring methods:

A

a-naphthly PO4

61
Q

If not assayed immediately, serum should be frozen or acidified to a pH lower than __

A

6.5

62
Q
  1. Prostatic Carcinoma
  2. Breast, Lung, Thyroid Carcinoma
  3. Gaucher’s Disease
  4. Niemann Pick Disease
A

Increased ACP

63
Q

More sensitive than Prostatic Acid Phosphatase in detecting stages A & B prostatic cancer:

A

Prostate-Specific Antigen

64
Q

Involved in the transfer of an amino group between aspartate and a-ketoacids with the formation of Oxaloacetate & Glutamate

A

Aspartate Aminotransferase

65
Q

Other name of AST:

A

Serum Glutamic Oxaloacetic Transaminase

66
Q

In AMI, AST levels:
1. Rise
2. Peak
3. Normalize

A
  1. 6-8 hours
  2. 24 hours
  3. 5 days
67
Q

Uses Malate Dehydrogenase and monitors the change in absorbance at 340 nm
Substrare: Oxaloacetate & Glutamate

A

Karmen Method
pH 7.5

68
Q

Catalyzes the transfer of an amino group from alanine to a-ketoglutarate with the formation of Glutamate & Pyruvate
Highest concentration in Liver
More Liver-Specific than AST

A

Alanine Aminotransferase

69
Q

Other name of ALT

A

Serum Glutamate-Pyruvate Transaminase

70
Q

ALT measurement is a more sensitive and specific screening test for ____ compared to AST

A

Posttransfusion Hepatitis or
Occupational Toxic Exposure

71
Q

Aminotransferases requires ___ as coenzymes

A

Pyridoxal Phosphate or
Vitamin B6

72
Q

Hemolysis should be avoided because it increases AST by:

A

10 times

73
Q

Method used for ALT:

A

Coupled Enzymatic Reaction
pH 7.5

74
Q

De Ritis Ratio

A

AST/ALT

75
Q

In children De Ritis ratio:

A

AST>ALT

76
Q

In adults, De Ritis Ratio:

A

ALT > AST

77
Q

De Ritis Ratio of:
1. < 1
2. > 1
3. 1-2
4. > 2

A
  1. Viral Hepatitis
  2. Nonviral origin Hepatic disease
  3. Hepatic Cirrhosis
  4. Alcoholism: Hepatocellular Carcinoma
78
Q

Catalyzes the breakdown of starch and glycogen
An important enzyme in the physiologic digestion of starch
Smallest enzyme in size
Earliest pancreatic marker

A

Amylase

79
Q

In AP, AMS levels:
1. Rise
2. Peak
3. Normalize

A
  1. 2-12 hours
  2. 24 hours
  3. 3-5 days
80
Q

Classic reference method expressed in Somogyi units
Measures the amount of reducing sugars produced by the hydrolysis of starch by the usual glucose method

A

Saccharogenic

81
Q

Measures amylase activity by following the decreases in substrate concentration

A

Amyloclastic

82
Q

Measures amylase activity by the increase in color intensity of the soluble dye-substrate solution

A

Chromogenic

83
Q

Measures amylase activity by a continuous-monitoring technique

A

Coupled-Enzyme Method

84
Q

Enzymes used for the Coupled-Enzyme fmethod for AMS:

A
  1. Amylase
  2. Glucosidase
  3. Hexokinase
  4. G-6-PD
85
Q

Normal Amylase/Creatinine Ratio:

A

1%-4%
0.01 - 0.04

86
Q

A:C Ratio in Acute Pancreatitis

A

(>) 4%
up to 15%

87
Q

A/C Ratio Formula:

A

(Urine AMS/Serum AMS) x (Serum crea/Urine Crea) x 100

88
Q

Enzyme that hydrolyzes the ester linkages of fats to produce alcohol and fatty acid
Catalyzes partial hydrolysis of dietary TAG in the intestine to the 2-monoglyceride intermediate
Most specific pancreatic marker

A

Lipase

89
Q

In AP, LPS levels:
1. Rise
2. Peak
3. Remains Elevated
4. Normalize

A
  1. 6 hours
  2. 24 hours
  3. 7 days
  4. 8-14 days
90
Q

In this disease, there are cell degradation that occurs and results into loss of amylase and lipase production

A

Chronic Pancreatitis

91
Q

Uses Olive Oil as substrate

A

Lipase Methods

92
Q

Hydrolysis of olive oil after incubation for 24 hours at 37C and titration of Fatty acids using NaOH
Substrate: 50% Olive Oik
End: Fatty Acid

A

Cherry Crandal Method
**Reference Method

93
Q

Most commonly used method
Does not use 50% Olive Oil

A

Peroxidase Coupling

94
Q

Enzyme that cataluzes the conversion of lactic and pyruvic acid
Zinc-containing enxymr that is part of glycolytic pathway
Has 5 Isoenzymes

A

Lactate Dehydrogenase

95
Q

Tissue Sources:

A
  1. Heart, RBCs, Kidneys - LD1 & LD2
  2. Lungs Pacnreas, Spleen - LD3
  3. Skeletal Muscles, Liver, Intestine - LD4 & LD5
96
Q

Highest LD levels are seen in what disease?

A

Pernicious anemia
Hemolytic Disorders

97
Q

In AMI, LD levels:
1. Rise
2. Peak
3. Elevated

A
  1. 12-24 hours
  2. 48-72 hours
  3. 10-14 days
98
Q

Hepatic Carcinoma & Toxic hepatitis will have __ increase

A

ten-fold

99
Q

In normal sera, LD pattern:

A

LD2 - LD1 - LD3- LD4 - LD5

100
Q

Flipped pattern (LD1>LD2) is seen in what diseasse?

A

Myocardial Infarction &
Hemolytic Anemia

101
Q

Reaction is at pH 8.8
Most commonly used method because it produces a positive rate and not affected by product inhibition

A

Wacker Method
Forward Method

102
Q

Reaction at pH 7.2
2x faster as the forward reaction
preferred method for dry slide tech

A

Wrobleuski La Due
Reverse method

103
Q

Cold-labile LD isoenzyme:

A

LD5

104
Q

Catalyzes the transfer of a phosphate group between creatine phosphate and adenosine diphosphate
Storage of High-energy creatine PO4 in the muscles

A

Creatine Kinase

105
Q

Most anodal, and Most labile CK isoenzyme

A

CK1

106
Q

Least Anodal CK

A

CK 3

107
Q

CK is a very sensitive indicator of what diseases?

A

Acute Myocardial Infarction &
Duchenne Diorder

108
Q

Highest elevation of total CK is seen in?

A

Duchenne’s Muscular Dystrophy
(50x)

109
Q

In AMI, CK levels:
1. Rise
2. Peak
3. Normalize

A
  1. 4-8 hours
  2. 12-24 hours
  3. 48-72 hours
110
Q

Done at pH 9.0
Forward reaction
Measures Creatine
Enzymes: CPK, PK, LD

A

Tanzer-Gilbarg Assay

111
Q

Most commonly used method
Faster reaction
pH 5.8
Reverse method
Measures Creatine Phosphate
EnzymeS: CPK, HK, G6PD

A

Oliver Rosalki Method

112
Q

Percentage of total CK that is attributed to CK-MB

A

CK Relative Index (CKI)

113
Q

Formula for CKI

A

(CK-MB/Total CK) x 100

114
Q

Glycolytic enzyme that splits Fructose-1,6-diphosphate into two triose phosphate molecules in the metabolism of glucose

A

Aldolase

115
Q

Isoenzymes of Aldolase:

A
  1. Aldolase A - Skeletal muscles
  2. Aldolase B - WBC, Liver, Kidney
  3. Aldolase C - Brain Tissue
116
Q

Phosphoric monoester hydrolase
Predominantly secreted from the liver
**Marker for HEPATOBILIARY DISEASE & INFILTRATIVE LESIONS OF THE LIVER

A

5’ Nucleotidase

117
Q

Catalyzes the transfer of glutamyl groups between peptides or amino acids through linkage as a gamma carboxyl group

A

Gamma Glutamyl Transaminase

118
Q

Useful in differentiating source of an increased ALP level
Elevated in all hepatobiliary disorders - biliary tract obstructions
Most sensitive marker for Acute Acoholic Hepatitis
Sensitive indicator of alcoholism

A

Gamma Glutamyl Transamine

119
Q

Secreted by liver, and reflects the Synthetic function of liver rather than hepatocyte injury
Catalyzes removal of benzyl group from cocaine
Marker for Insecticide/Pesticide poisoning

A

Pseudocholinesterase

120
Q

Also known as Peptidyldipeptidase A or Kininase II
Converts Angiotensin 1 to Angiotensin 2 within lungs
Critical target for inhibitory drugs designed to lower blood pressure

A

Angiotensin-Converting Enzyme

121
Q

Also a marker for hepatobiliary diseases:

A

Ornithine Carbamoyl Transferase (OCT)

122
Q

Functions to maintain NADPH in the reduced form in the erythrocytes
Newborn screening marker
Deficiency can lead to drug-induced hemolytic anemia after taking primaquine (anti-malarial drug)

A

Glucose-6-Phosphate Dehydrogenase

Clinical Chemistry (16 decks)

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