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[LAB] CC2 > [M1] Enzyme Methodologies > Flashcards

[M1] Enzyme Methodologies Flashcards

1
Q

Liver enzymes is also called as

A

Hepatic enzymes

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2
Q

Enumerate the Liver Enzymes

A

Alkaline Phosphatase
Aspartate Aminotransferase
Alanine Aminotransferase
Gamma-Glutamyltransferase
5’-Nucleotidase

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3
Q

ALP

A

ALKALINE PHOSPHATASE

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4
Q

E.C OF ALP

A

E.C. 3.1.3.1

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5
Q

Catalyze the hydrolysis of phosphomonoesters at an alkaline pH (9.0-10.0)

A

ALKALINE PHOSPHATASE

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6
Q

ALP catalyzes the hydrolysis of _________________ at an (acidic/alkaline) pH (_____________)

A

ALP

phosphomonoesters
alkaline
9.0-10.0

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7
Q

Common name of ALP

A

alkaline orthophosphoric monoester phosphohydrolase

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8
Q

ALP

Function:
remove (organic/inorganic) phosphate from an (organic/inorganic) phosphate ester with the concomitant production of ___________

A

inorganic
organic
alcohol

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9
Q

T/F: ALP is a non-specific enzyme

A

T

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10
Q

Activators of ALP

A

Mg2+
Co2+
Mn2+

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11
Q

inhibitors of ALP

A

phosphate
borate
oxalate

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12
Q

ALP is useful for evaluation of ___________ and ________ disorders

A

hepatobiliary
bone

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13
Q

RF of ALP in 20-50 MALE

A

53-128 U/L

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14
Q

RF of ALP in 20-50 FEMALE

A

42-98 U/L

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15
Q

RF of ALP in ≥60 MALE

A

56-119 U/L

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16
Q

RF of ALP in ≥60 FEMALE

A

53-141 U/L

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17
Q

RF of ALP in 4-15

A

54-369 U/L

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18
Q

What are the major ALP isoenzymes

A

Liver ALP
Bone ALP
Placental ALP
Intestinal ALP

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19
Q

Half life of Liver ALP

A

3 days

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20
Q

Half life of Bone ALP

A

1 day

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21
Q

Half life of Placental ALP

A

7 days

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22
Q

Half life of Intestinal ALP

A

1 day

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23
Q

Rank the ALP isoenzymes from most ANODAL to least ANODAL

A
  1. Liver ALP
  2. Bone ALP
  3. Placental ALP
  4. Intestinal ALP
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24
Q

Rank the ALP isoenzymes from most CATHODAL to least CATHODAL

A
  1. Intestinal ALP
  2. Placental ALP
  3. Bone ALP
  4. Liver ALP
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25
Q

Rank the ALP isoenzymes from most heat stable to least heat stable

A
  1. Placental ALP
  2. Intestinal ALP
  3. Liver ALP
  4. Bone ALP
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26
Q

Rank the ALP isoenzymes from most heat-labile to least heat-labile

A
  1. Bone ALP
  2. Liver ALP
  3. Intestinal ALP
  4. Placental ALP
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27
Q

inhibitor of Liver ALP

A

Levamisole

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28
Q

inhibitor of Bone ALP

A

Levamisole &
3M urea

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29
Q

Inhibitor of Placental ALP

A

Phenylalanine

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30
Q

Inhibitor of Intestinal ALP

A

Phenylalanine

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31
Q

BEFORE HEAT

Placental ALP
Liver ALP
Bone ALP

A

100%
100%
100%

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32
Q

AFTER HEAT

Placental ALP
Liver ALP
Bone ALP

A

100%
>20%
<20%

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33
Q

Heat Fractionation/ Stability Test is measured @ ____ for ____ minutes

A

56°C
10 minutes

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34
Q

T/F: ALP isoenzymes are NOT measured before and after heating

A

F; Measured before and after heating

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35
Q

separates liver and bone ALP

A

Neuraminidase
Wheat Germ Lectin

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36
Q

Steps in Heat Fractionation/ Stability Test

A
  1. Measure ALP
  2. Heat sample @ 56°C for 10 minutes
  3. Measure ALP
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37
Q

Heating sample @ 56°C for 10 minutes significance

A

To inactivate other isoenzymes

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38
Q

Abnormal ALP isoenzyme associated with neoplasms or cancer

A

Carcinoplacental ALPs

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39
Q

Carcinoplacental ALPs

Abnormal ALP isoenzyme associated with __________ or _________

A

neoplasms
cancer

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40
Q

2 types of Carcinoplacental ALPs

A

Regan ALP
Nagao ALP

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41
Q

Detected in gynecological CA (ovarian, breast), lung CA, and colon CA.

A

Regan ALP

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42
Q

Regan ALP

Detected in ________ (ovarian, breast), ___ CA, and ____ CA.

A

gynecological CA
lung CA
colon CA

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43
Q

Migrates to the same position as the Bone ALP

A

Regan ALP

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44
Q

Regal ALP migrates to the same position as ___________

A

Bone ALP

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45
Q

Most heat stable ALP isoenzyme

A

Regan ALP

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46
Q

T/F: Regan ALP is more heat stable than placental ALP

A

T

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47
Q

Regan ALP is stable @ ______for ____minutes

A

65°C
30

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48
Q

Inhibitor of Regan ALP

A

phenylalanine

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49
Q

Detected in metastatic carcinoma of pleural surfaces, and adenocarcinoma of pancreas and bile ducts

A

Nagao ALP

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50
Q

Nagao ALP

Detected in _______________ of pleural surfaces, and ____________ of pancreas and bile ducts

A

metastatic carcinoma
adenocarcinoma

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51
Q

Nagao ALP

Detected in metastatic carcinoma of _________________, and adenocarcinoma of _______ and _________

A

pleural surfaces
pancreas and bile ducts

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52
Q

Variant of Regan ALP

A

Nagao ALP

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53
Q

Inhibitor of Nagao ALP

A

phenylalanine
L-Leucine

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54
Q

Method of Analysis for ALP

A

Bowers and McComb

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55
Q

A continuous monitoring method allowing calculation of ALP activity based on the molar absorptivity of _________________

A

BOWERS AND MCCOMB

p-nitrophenol

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56
Q

The most specific method; IFCC recommended method

A

Bowers and McComb

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57
Q

Enumerate the Other Methodologies for ALP

A
  1. Bodansky
  2. Shinowara
  3. Jones
  4. Reinhart
  5. King and Armstrong
  6. Bessy, Lowry, and Brock
  7. Bowers and McComb
  8. Huggins and Talalay
  9. Moss
  10. Klein, Babson and Read
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58
Q

Substrate for

  1. Bodansky
  2. Shinowara
  3. Jones
  4. Reinhart
A

Beta-Glycerol Phosphate

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59
Q

End Product for

  1. Bodansky
  2. Shinowara
  3. Jones
  4. Reinhart
A

Inorganic phosphate + glycerol

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60
Q

Substrate for King and Armstrong

A

Phenylphosphate

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61
Q

End product for King and Armstrong

A

Phenol

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62
Q

Substrate for

  1. Bessy, Lowry, and Brock
  2. Bowers and McComb
A

p-nitrophenyl phosphate

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63
Q

End product for

  1. Bessy, Lowry, and Brock
  2. Bowers and McComb
A

p-nitrophenol/
yellow nitrophenoxide ion

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64
Q

Substrate for Huggins and Talalay

A

Phenolphthalein phosphate

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65
Q

End product for Huggins and Talalay

A

Phenolphthalein red

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66
Q

Substrate for Moss

A

Alpha-naphthol phosphate

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67
Q

End product for Moss

A

Alpha-naphthol

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68
Q

Substrate for Klein, Babson, and Read

A

Buffered phenolphthalein phosphate

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69
Q

End product for Klein, Babson, and Read

A

Free phenolphthalein

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70
Q

False Increase of ALP

A

Hemolysis
Diet (Fatty meals)
Stored at low temperature (4°C)

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71
Q

FALSE INC. IN ALP

Hemolysis - ALP in RBC is ___ more concentrated than serum or plasma

A

6x

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72
Q

FALSE INC. IN ALP

Diet (fatty meals) - ALP is ____ higher

A

25%

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73
Q

Diagnostic Significance of ALP

ALP - #1 marker in ______________

A

obstructive jaundice

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74
Q

Increased ALP

A

● Osteitis deformans
● Obstructive Jaundice
● Osteomalacia
● Rickets
● Osteoblastic bone tumors
● Sprue
● Hyperparathyroidism
● Hepatitis and Cirrhosis

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75
Q

Osteitis deformans is also known as

A

“Paget’s disease”

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76
Q

AST

A

ASPARTATE AMINOTRANSFERASE

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77
Q

E.C of ASPARTATE AMINOTRANSFERASE

A

E.C. 2.6.1.1

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78
Q

Old name of ASPARTATE AMINOTRANSFERASE

A

Serum Glutamic
Oxaloacetate Transaminase

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79
Q

ASPARTATE AMINOTRANSFERASE

Catalyze the transfer of amino groups
between _________ (substrate) and
___________

A

aspartate
a-ketoacids

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80
Q

ASPARTATE AMINOTRANSFERASE

Catalyze the transfer of amino groups
between aspartate (substrate) and
a-ketoacids with the formation of
________ and ___________

A

oxaloacetate
glutamate

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81
Q

ASPARTATE AMINOTRANSFERASE

Coeznyme

A

Pyridoxal phosphate

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82
Q

ASPARTATE AMINOTRANSFERASE

Major Tissue Source

A

Cardiac tissues
liver and skeletal muscle

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83
Q

ASPARTATE AMINO TRANSFERASE

RR

A

5-35 U/L

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84
Q

ASPARTATE AMINOTRANSFERASE

Isozenzymes

A

Cytoplasmic AST
Mitochondrial AST

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85
Q

Predominant in the circulation of a healthy
individual

A

Cytoplasmic AST

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86
Q

Method of Analysis for AST

A

Karmen Method

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87
Q

Karmen Method is what type of enzymatic method

A

Coupled enzymatic method

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88
Q

Indicator enzyme for Karmen method

A

Malate
dehydrogenase (MD)

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89
Q

KARMEN METHOD (AST)

It monitors the (increase/decrease) in
absorbance at _____ nm

A

decrease
340

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90
Q

KARMEN METHOD (AST)

Storage: stable for ____ days at __________

A

3-4
refrigerated temp.

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91
Q

Variables for Karmen Method

A

Hemolysis

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92
Q

Hemolysis in Karmen Method results in false (increase/decrease) up to ___

A

increase
10x

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93
Q

Exhibits highest level AST

A

Acute Hepatocellular Disorder

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94
Q

ALT

A

ALANINE AMINOTRANSFERASE

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95
Q

E.C OF ALANINE AMINOTRANSFERASE

A

● E.C 2.6.1.2

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96
Q

old name for Alanine Aminotransferase

A

Serum Glutamic Pyruvic Transaminase

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97
Q

ALANINE AMINOTRANSFERASE

Catalyze transfer of amino group
between _________ (substrate) and
______________

A

alanine
a-ketoglutarate

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98
Q

ALANINE AMINOTRANSFERASE is significant in the evaluation of what disorders

A

Hepatic disorders

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99
Q

ALANINE AMINOTRANSFERASE (ALT)

Coenzyme

A

Pyridoxal phosphate

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100
Q

ALANINE AMINOTRANSFERASE (ALT)

Major Tissue Source

A

Liver

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101
Q

ALANINE AMINOTRANSFERASE (ALT)

RR

A

7-45 U/L

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102
Q

Method of Analysis for ALANINE AMINOTRANSFERASE (ALT)

A
  1. Coupled Enzymatic Method
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103
Q

ALT

Indicator Enzyme for Coupled Enzymatic Method

A

Lactate Dehydrogenase (LDH)

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104
Q

Coupled Enzymatic Method (ALT)

The change in absorbance at ______ nm
measured ________________ is directly
proportional to ALT activity (pH
_________).

A

340
continuously
7.3-7.8

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105
Q

Coupled Enzymatic Method (ALT)

Storage

A

3-4 days at 4°C

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106
Q

T/F: Hemolysis does NOT affect ALT

A

True

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107
Q

Increase Aminotransferases (AST, ALT)

A
  1. Toxic Hepatitis
  2. Acute Myocardial Infarction (AST)
  3. Wolff-Parkinson White Syndrome
  4. Trichinosis (AST)
  5. Chronic alcoholism
  6. Dermatomyositis
  7. Hepatic cancer
  8. Reye’s Syndrome
  9. Viral Hepatitis
  10. Muscular dystrophy (AST)
  11. Acute pancreatitis (AST)
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108
Q

Which disorders/diseases causes Increase in AST only

A

Acute Myocardial Infarction (AST)
Trichinosis (AST)
Muscular dystrophy (AST)
Acute pancreatitis (AST)

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109
Q

Acute Myocardial Infarction (AST)

Rise
Peak
Normal

A

6-8 hours
24 hours
within 5 days

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110
Q

Trichinosis is caused by

A

Trichinella spiralis

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111
Q

unknown source in GGT is caused by pancreas

A

Acute pancreatitis

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112
Q

AST/ALT ratio

A

DE RITIS RATIO

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113
Q

Used to differentiate the cause
of hepatic disorder

A

DE RITIS RATIO

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114
Q

DE RITIS RATIO

> 1: __________

A

non-viral cause

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115
Q

DE RITIS RATIO

<1: __________

A

viral

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116
Q

GGT

A

GAMMA-GLUTAMYLTRANSFERASE

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117
Q

E.C of GAMMA-GLUTAMYLTRANSFERASE

A

E.C. 2.3.2.2

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118
Q

GAMMA-GLUTAMYLTRANSFERASE catalyzes ____________________

A

transpeptidation

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119
Q

The transfer of ɣ-glutamyl residue
from ɣ-glutamyl peptides to amino
acids, water and other peptides

A

transpeptidation

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120
Q

Used for diagnosis of hepatobiliary
disorders and alcoholism

A

GAMMA-GLUTAMYLTRANSFERASE
(GGT)

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121
Q

GAMMA-GLUTAMYLTRANSFERASE
(GGT) is sed for diagnosis of _____________
and _____________

A

hepatobiliary disorders
alcoholism

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122
Q

Useful for differentiating source of
serum ALP elevation

A

GAMMA-GLUTAMYLTRANSFERASE
(GGT)

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123
Q

LIVER DISORDER

ALP
GGT

A

Increased
Increased

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124
Q

BONE DISEASE

ALP
GGT

A

Increased
Normal

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125
Q

Critical for the intracellular
maintenance of reduced glutathione

A

GAMMA-GLUTAMYLTRANSFERASE
(GGT)

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126
Q

GAMMA-GLUTAMYLTRANSFERASE (GGT)

Tissue source

A

Liver (epithelial cell lining of biliary ducts and bile canalicular)
Kidneys
Brain
Pancreas,
Intestine
Prostate.

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127
Q

Method of Analysis for GAMMA-GLUTAMYLTRANSFERASE (GGT)

A

Szasz Assay

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128
Q

Method for Szasz Assay

A

Fixed-point or continuous monitoring

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129
Q

Szasz Assay

Substrate

A

γ-glutamyl-p-nitroanilide

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130
Q

Szasz Assay

End product

A

p-nitroaniline

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131
Q

Szasz Assay

wavelength

A

405-420 nm

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132
Q

Szasz Assay

Preferred specimen

A

Serum
EDTA Plasma

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133
Q

Szasz Assay

Storage:

A

4°C (1 week)
-20°C (1 month)

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134
Q

Other Method for GGT

A

Rosalki and Tarrow, Orlowski

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135
Q

T/F; GGT is not effected by hemolysis

A

T

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136
Q

Why is GGT not affected by hemolysis?

A

GGT is not found in RBC

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137
Q

GGT

RR: Male

A

6-55 U/L

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138
Q

GGT

RR: female

A

5-38 U/L

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139
Q

Most sensitive marker of acute
alcoholic hepatitis

A

GAMMA-GLUTAMYLTRANSFERASE
(GGT)

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140
Q

Normal levels in patients with bone
disease and during pregnancy

A

GAMMA-GLUTAMYLTRANSFERASE
(GGT)

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141
Q

GGT

Normalize: ___ weeks after consumption

A

2-3

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142
Q

5’N

A

5’-NUCLEOTIDASE

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143
Q

E.C. of 5’-NUCLEOTIDASE

A

E.C. 3.1.3.5

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144
Q

5’-NUCLEOTIDASE

Other name

A

5’ ribonucleotide phosphohydrolase

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145
Q

A phosphoric monoester hydrolase
reacting only on nucleoside-5’-phosphates (_______,
__________) releasing (inorganic/organic) phosphate

A

5’-NUCLEOTIDASE

AMP
adenylic acid
inorganic

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146
Q

5’-NUCLEOTIDASE

Major Source

A

Liver

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147
Q

Marker of hepatobiliary disease and
infiltrative lesions of the liver

A

5’-NUCLEOTIDASE

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148
Q

5’-NUCLEOTIDASE

Marker of _____________ and
____________________ of the liver

A

hepatobiliary disease
infiltrative lesions

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149
Q

Secondary Marker for Obstructive Jaundice

A

5’-NUCLEOTIDASE

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150
Q

Method for 5’-NUCLEOTIDASE

A

Dixon & Purdon
Campbell
Belfield & Goldberg

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151
Q

Method for 5’-NUCLEOTIDASE

A

Dixon & Purdon
Campbell
Belfield & Goldberg

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152
Q

5’-NUCLEOTIDASE

RR

A

0-1.6 U/L

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153
Q

5’-NUCLEOTIDASE

Storage

A

4°C (4 days)
-20°C (4 months)

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154
Q

Enumerate the Pancreatic Enzymes

A
  1. Amylase
  2. Lipase
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155
Q

AMS

A

Amylase

156
Q

E.C for Amylase

A

E.C. 3.2.1.1

157
Q

AMYLASE

Other name

A

alpha-1,4-glucan-4-glucohydrolase

158
Q

AMYLASE

Catalyzes the hydrolysis of __________________ in
polysaccharides (_____, _____)

A

𝛂-1,4-glycosidic bonds
starch, glycogen

159
Q

Earlier pancreatic marker

A

Amylase

160
Q

Smallest enzyme (freely filtered by the
_________)

A

AMYLASE

glomerulus

161
Q

AMYLASE

Activators

A

Calcium, Chloride

162
Q

AMYLASE

Major Tissue Source

A

Pancreas (acinar cells)
Salivary Glands

163
Q

AMYLASE (AMS)

RR; Serum

A

28-100 U/L

164
Q

AMYLASE (AMS)

RR; Urine

A

1-15 U/h

165
Q

Enumerate the isoenzymes of Amylase

A
  1. S-type/Ptyalin/Salivary
  2. P-type / Amylopsin / Pancreatic
166
Q

↑ parotitis/mumps

A
  1. S-type/Ptyalin/Salivary
167
Q

The most anodal AMY isoenzyme

A
  1. S-type/Ptyalin/Salivary
168
Q

S-type/Ptyalin/Salivary is secreted by __________________

A

salivary glands

169
Q

Inhibitor of S-type/Ptyalin/Salivary (inhibits activity of salivary glands)

A

Wheat Germ Lectin

170
Q

↑ in acute pancreatitis

A

P-type / Amylopsin / Pancreatic

171
Q

the most predominant subtype of P-type / Amylopsin / Pancreatic

A

P3

172
Q

● Secreted by the pancreas and also by
the fallopian tube & lungs

A

P-type / Amylopsin / Pancreatic

173
Q

T/F: In the laboratory, we measure the Total Amylase

A

TRUE

174
Q

Specimen for Amylase

A

Serum,
Heparinized Plasma

175
Q

Substrate for Amylase

A

Starch

176
Q

Enumerate the different Method of Analysis of Amylase

A
  1. Saccharogenic
  2. Amyloclastic
  3. Chromogenic
  4. Coupled-Enzyme
177
Q

AMYLASE

Classic reference method

A

Saccharogenic

178
Q

It measures the amount of __________ produced by the hydrolysis of ______ by the usual glucose method

A

SACCHAROGENIC

reducing sugars
starch

179
Q

Enumerate the glucose methods used in Saccharogenic

A

Hexokinase
Glucose oxidase

180
Q

Glucose methodology reference method

A

Hexoklnase

181
Q

End product for Saccharogenic

A

Glucose

182
Q

AMYLASE

inverse method

A

Amyloclastic

183
Q

It measures decrease in starch substrate

A

Amyloclastic

184
Q

Amyloclastic

Substrates are coupled with_____

A

iodine

185
Q

Iodine + Starch = _____________

A

Dark-blue color

186
Q

Why Dark Blue Color in Amyloclastic?

A

e iodine is trapped
within the structure of the starch

187
Q

T/F: In amyloclastic, decrease in color is proportional to AMS activity

A

T

188
Q

Measures the formation of soluble
starch fragments coupled with
chromogenic dyes.

A

Chromogenic

189
Q

Color intensity is proportional to AMS
activity

A

Chromogenic

190
Q

Measured amylase activity by a continuous-monitoring/kinetic technique.

A

Coupled-Enzyme

191
Q

Substrate for Couple-Enzyme (Amylase)

A

Starch

192
Q

Wavelength for Couple-Enzyme (Amylase)

A

340 nm

193
Q

pH for Couple-Enzyme (Amylase)

A

6.9

194
Q

Storage for Couple-Enzyme (Amylase)

A

Room temp (1 week)
4°C (2 months)

195
Q

False Decrease in AMS

A

● Ca2+ Chelating Anticoagulant
● Triglycerides

196
Q

False Increase in AMS

A

● Morphine, other opiates

197
Q

amylase bound to immunoglobulin

A

Macroamylasemia

198
Q

asymptomatic amylasemia

A

Macroamylasemia

199
Q

In Macroamylasemia, (increase/decrease) serum AMS & (increase/decrease) N Urine AMS

A

Increase
Decrease

200
Q

↑ serum AMS & ↑ urine AMS

A

Hyperamylasemia

201
Q

Amylase/Creatinine Ratio:

Normal

A

1-4% (0.01-0.04)

202
Q

Amylase/Creatinine Ratio:

Acute Pancreatitis

A

> 4%-15%

203
Q

LPS

A

Lipase

204
Q

E.C of Lipase

A

E.C. 3.1.1.3

205
Q

LIPASE

Other name

A

Triacylglycerolacylhydrolase

206
Q

Catalyzes hydrolysis of glycerol esters
of complex lipids to produce ___________
and ________.

A

LIPASE

alcohol
fatty acid.

207
Q

Catalyzes partial hydrolysis of ________ to________________,
with production of long-chain fatty
acids.

A

LIPASE

dietary TAG
2-monoglyceride intermediate

208
Q

More pancreatic specific

A

LIPASE

209
Q

LIPASE

Cofactor

A

Colipase (coenzyme)
Bile salts

210
Q

LIPASE

Major Tissue Source

A

Pancreas

211
Q

LIPASE

RR

A

<38 U/L

212
Q

Method of Analysis for Lipase

Specimen

A

Serum

213
Q

Method of Analysis for Lipase

Storage

A

room temp (1 week)
4°C (3 weeks)

214
Q

Method of Analysis for Lipase

Interferences

A

Hemolysis

215
Q

Enumerate the Methods for Lipase

A
  1. Cherry-Crandall
  2. Tietz
  3. Peroxidase Coupling
216
Q

Substrate for Cherry-Crandall and Tietz

A

50% Olive oil (Triolein)

217
Q

Titrating Agent for Cherry-Crandall and Tietz

A

0.4N NaOH

218
Q

Indicator for Cherry-Crandall

A

Phenolphthalein

219
Q

Indicator for Tietz

A

Thymolphthalein + Veronal

220
Q

Endpoint for Cherry-Crandall and Tietz

A

Fatty Acids (Oleic acid)

221
Q

End color of Cherry-Crandall

A

Pink

222
Q

End color of Tietz

A

Blue

223
Q

Most commonly used method (LPS)

A

Peroxidase Coupling

224
Q

Does not use 50% olive oil (LPS)

A

Peroxidase Coupling

225
Q

most specific pancreatic marker

A

Lipase

226
Q

In chronic pancreatitis:
→ _____________ are destroyed
→ Loss of_____ and _____

A

Acinar cells
AMS and LPS

227
Q

AMYLASE

Rise
Peak
Normalize

A

5-8 HOURS
24 HOURS
3-5 DAYS

228
Q

LIPASE

Rise Peak Normalize

A

4-8 HOURS
24 HOURS
8-14 DAYS

229
Q

Enumerate the Cardiac Markers

A
  1. Creatine Kinase
  2. Lactate Dehydrogenase
230
Q

CK

A

Creatine Kinase

231
Q

E.C for Creatine Kinase

A

● E.C. 2.7.3.2

232
Q

CREATINE KINASE

Other Name

A

ATP-Creatine-N-phosphotransferase

233
Q

Catalyzes phosphorylation of creatine
to form _____________

A

CREATINE KINASE

creatine phosphate.

234
Q

Involved in the storage of high-energy
creatine phosphate in ___________

A

CREATINE KINASE

muscle cells

235
Q

contains two subunits

A

CREATINE KINASE

Dimeric Molecule

236
Q

2 subunits of CREATINE KINASE

A

→ M subunit (Muscle)
→ B subunit (Brain)

237
Q

CREATINE KINASE

Major Tissue Source

A

brain
muscles (smooth, skeletal, cardiac)

238
Q

CREATINE KINASE

RR: Male

A

46-171 U/L

239
Q

CREATINE KINASE

RR: Female

A

35-145 U/L

240
Q

CREATINE KINASE

RR: CK-MB

A

<5% of total CK

241
Q

Enumerate the Normal Isoenzymes of Creatine Kinase

A

CK-BB
CK-MB
CK-MM

242
Q

Rank the CK isoenzymes from most ANODAL to least ANODAL

A
  1. CK-BB
  2. CK-MB
  3. CK-MM
243
Q

Rank the CK isoenzymes from most CATHODAL to least CATHODAL

A
  1. CK-MM
  2. CK-MB
  3. CK-BB
244
Q

Brain type CK Isoenzyme

A

CK-BB

245
Q

Hybrid type CK Isoenzyme

A

CK-MB

246
Q

Muscle type CK Isoenzyme

A

CK-MM

247
Q

Dominant in brain, intestines, and smooth muscles

A

CK-BB

248
Q

CK-BB is dominant in:

A

brain
intestines
smooth muscles

249
Q

Present in significant concentration in the cardiac
muscles

A

CK-MB

250
Q

CK-MB is present in significant concentration in the ___________________

A

cardiac muscles

251
Q

Abundantly present in striated muscles

A

CK-MM

252
Q

CK-MM is abundantly present in _________

A

striated muscles

253
Q

Rarely found in Serum

A

CK-BB

254
Q

Why is CK-BB rarely found in serum?

A

it cannot pass through the blood-brain barrier

255
Q

Serodiagnostic tool for AMI

A

CK-MB

256
Q

Major Isoenzyme in normal
individual (______)

A

CK-MM

94-100%

257
Q

Useful Non-Specific Tumor Marker

A

CK-BB

258
Q

RV of CK-MB

A

<5% of Total CK

259
Q

Myocardial Damage/AMI:

A

● Elevated CK-MB
● >6 of Total CK

260
Q

earliest enzymatic cardiac marker

A

CK-MB

261
Q

increased CREATINE KINASE

A
  1. Acute Myocardial Infarction
  2. Duchenne-type Muscular Dystrophy
  3. Rhabdomyolysis
  4. Cerebrovascular Accident
  5. Seizures
  6. Nerve Degeneration
  7. CNS Shock
  8. Hypothyroidism
  9. Malignant Hyperpyrexia
  10. Reye’s Syndrome
262
Q

Highest elevation of total CK

A

Duchenne-type Muscular Dystrophy

263
Q

Method of Analysis for CK

Specimen

A

Serum
Heparinized Plasma

264
Q

Inhibitor of sulfhydryl group oxidation

A

→ N-acetylcysteine
→ Mercaptoethanol
→ Thioglycerol
→ Dithiothreitol

265
Q

T/F: Serum activity in CK is stable

A

FALSE; VERY UNSTABLE

266
Q

Why is serum in CK very unstable?

A

because it is easily be inactivated by sulfhydryl
group by oxidation

267
Q

Variables for CK

A

Hemolysis
Light
Non-heparinized Anticoagulant
Physical Activity
IM Injection

268
Q

VARIABLES FOR CK

Hemolysis hgb level

A

> 320 mg/L HGB

269
Q

Total CK in Hemolysis is falsely elevated due to ______________ (enzyme) that is present in RBC

A

Adenylate kinase

270
Q

To prevent false elevation because of adenylate kinase, add __________________

A

Adenosine monophosphate

271
Q

Why is light a variable in CK

A

because CK is inactivated if exposed to light

272
Q

Methods for CK

A
  1. Tanzer-Gilvarg Assay
  2. Oliver-Rosalki Method
273
Q

Methods for CK

Forward/Direct Method

A
  1. Tanzer-Gilvarg Assay
274
Q

Tanzer-Gilvarg Assay is coupled with _______________________________________________

A

pyruvate kinase-lactate dehydrogenase-NADH system

275
Q

Tanzer-Gilvarg Assay

Optimal pH

A

9.0

276
Q

Tanzer-Gilvarg Assay

Wavelength

A

340 nm

277
Q

Methods for CK

Reverse/indirect Method

A

Oliver-Rosalki Method

278
Q

Most commonly performed method for CK

A

Oliver-Rosalki Method

279
Q

Oliver-Rosalki Method is couple with _______________________________________________________

A

Hexokinase-Glucose-6- Phosphate-Dehydrogenase-NADP system

280
Q

Oliver-Rosalki Method

Optimal pH

A

6.8

281
Q

Oliver-Rosalki Method

Wavelength

A

340 nm

282
Q

LDH

A

Lactate Dehydrogenase

283
Q

E.C of Lactate Dehydrogenase

A

E.C. 1.1.1.27

284
Q

Catalyze the interconversion (reversible) of ________ and __________

A

LACTATE DEHYDROGENASE

lactic acid
pyruvic acid

285
Q

LDH

Coenzyme

A

NAD+

286
Q

LDH

Inhibitor

A

Ethylenediamine tetraacetic acid (EDTA)

287
Q

contain A-peptide or M-peptide unit

A

LACTATE DEHYDROGENASE

Tetrametic Molecule

288
Q

● Widely distributed

A

LACTATE DEHYDROGENASE (LDH)

289
Q

LDH

Highest Activity

A

Heart
RBCs
skeletal muscles

290
Q

LDH

RV

A

125-220 u/L

291
Q

Enumerate the LDH Isoenzymes

A

LD 1
LD 2
LD 3
LD 4
LD 5
LD 6

292
Q

Most predominant LDH isoenzyme

A

LD 2

293
Q

increased in pulmonary involvement and various
carcinomas

A

LD3

294
Q

LD3 is increased in ______________ and _____________________

A

pulmonary involvement
various carcinomas

295
Q

LDH Isoenzyme

Seen in muscular injuries

A

LD 4

296
Q

LD 6 a.k.a

A

Alcohol dehydrogenase

297
Q

Present in Arteriosclerotic cardiovascular failure

A

LD 6

298
Q

LD6 is present in _________________________

A

Arteriosclerotic cardiovascular failure

299
Q

SUBUNITS

LD 1
LD 2
LD 3
LD 4
LD 5
LD 6

A

HHHH
HHHM
HHMM
HMMM
MMMM
none

300
Q

Tissue source of LD 1

A

Heart, RBC

301
Q

Tissue source of LD 2

A

Heart, RBC

302
Q

Tissue source of LD 3

A

Liver
Spleen,
Lymphocytes
Pancreas

303
Q

Tissue source of LD 4

A

Liver

304
Q

Tissue source of LD 5

A

Skeletal muscle

305
Q

Percentage based on Total LDH

LD 1

A

14-26%

306
Q

Percentage based on Total LDH

LD 2

A

29-39%

307
Q

Percentage based on Total LDH

LD 3

A

20-26%

308
Q

Percentage based on Total LDH

LD 4

A

8-16%

309
Q

Percentage based on Total LDH

LD 5

A

6-16%

310
Q

used as tumor markers

A

LD 2
LD 3
LD 4

311
Q

LD2, LD3, LD4 -used as tumor markers for:

A

→ acute leukemia
→ germ cell tumor
→ breast cancer
→ lung cancer

312
Q

Most to least dominant cases of: (Descending Order)

Normal Pattern

A

LD 2>1>3>4>5

313
Q

Method of Analysis LDH

Specimen

A

Serum

314
Q

Method of Analysis LDH

Substrate

A

→ Lactate
→ Pyruvate
→ α-hydroxybutyrate (LD1)

315
Q

Method of Analysis LDH

Storage: Total LD

A

25°C (48 hours)

316
Q

Method of Analysis LDH

Storage: LD isoenzymes

A

25°C (24 hours)

317
Q

Variables for LDH

A

→ Plasma specimen
→ Hemolysis
→ Cold storage

318
Q

Plasma specimen and Hemolysis in LDH causes false (increase/decrease) because of the presence of ____________

A

increase
plaelets

319
Q

Cold Storage of LDH causes false (increase/decrease) in _____ and _____

A

Decrease
LD 4 and LD 5

320
Q

Enumerate the methods used in LDH

A
  1. Wacker Method
  2. Wrobleuski La Due
321
Q

Method of Analysis LDH

Forward/Direct Method

A

Wacker Method

322
Q

Method of Analysis (LDH)\

Most commonly used method

A

Wacker Method

323
Q

pH in Wacker Method

A

8.3-8.9

324
Q

Wavelength in Wacker Method

A

340 nm

325
Q

Method of Analysis LDH

Reverse/Indirect Method

A

Wrobleuski La Due

326
Q

Wrobleuski La Due is ____ the rate of forward method

A

thrice

327
Q

● Preferred Method for Dry-Slide
Technology

A

Wrobleuski La Due

328
Q

Example of Dry-Slide Techbology

A

Vitros Analyzer

329
Q

Uses less costly cofactor and it has a
smaller specimen volume requirement

A

Wrobleuski La Due

330
Q

Wrobleuski La Due

pH

A

7.1-7.4

331
Q

Increased LDH

A
  1. Acute Myocardial Infarction
  2. Hemolytic anemia
  3. Pernicious anemia
  4. Pulmonary infarction
  5. Muscle dystrophy
  6. Hepatic carcinoma, toxic hepatitis,
    cirrhosis, viral hepatitis
  7. Blood transfusion
  8. Pneumocystis jirovecii infection
332
Q

INCREASED LDH

Acute Myocardial Infarction exhibits what type of pattern

A

→ Flipped pattern
→ LD 1>2>3>4>5

333
Q

INCREASED LDH

Pulmonary Infarction exhibits what pattern

A

LD 3>4>2>1>5

334
Q

INCREASED LDH

Muscle dystrophy what pattern

A

LD 5>4>3>2>1

335
Q

Which disorders/diseases in Increased LDH exhibits increased LD 4

A

Hepatic carcinoma, toxic hepatitis,
cirrhosis, viral hepatitis

336
Q

__ & __ = LD is increased but normalize after ______

A

6 and 7
24 hours

337
Q

T/F: Increase in Total LDH is insignificant

A

T

338
Q

Why is an increase in Total LDH insignificant?

A

because LDH is present almost virtually in cells

339
Q

Acute Myocardial infarction

______ of total CK ______

A

> 6%
1:20:0

340
Q

Acute Myocardial infarction

Enumerate the Enzymes involved

A

Aspartate Aminotransferase
Creatine Kinase-MB
Lactate Dehydrogenase

341
Q

ACUTE MYCOCARDIAL INFARCTION

Enzyme not liver specific

A

Aspartate aminotransferase

342
Q

ACUTE MYOCARDIAL INFARCTION

Enzyme cardiac specific

A

Creatine Kinase-MB

343
Q

ASPARTATE AMINOTRANSFERASE

Rise
Peak
Normalize

A

6-8 hours
24 hours
Within 5 days

344
Q

CREATINE KINASE-MB

Rise
Peak
Normalize

A

4-8 hours ‘
12-24 hours
48-72 hours

345
Q

LACTATE DEHYDROGENASE

Rise
Peak
Normalize

A

12-24 hours
48-72 hours
After 10-14 days

346
Q

Enumerate the other Clinically Significant Enzymes

A
  1. Acid Phosphatase
347
Q

ACP

A

Acid Phosphatase

348
Q

E.C of ACID PHOSPHATASE

A

E.C. 3.1.3.2

349
Q

ACID PHOSPHATASE

Other name

A

Acid orthophosphoric
monoester phosphohydrolase

350
Q

Catalyze the hydrolysis of phosphomonoesters at an acidic pH

A

ACID PHOSPHATASE (ACP)

351
Q

ACID PHOSPHATASE

Major Tissue Source

A

Prostate

352
Q

Useful for evaluation of metastatic-prostatic carcinoma

A

ACID PHOSPHATASE (ACP)

353
Q

ACID PHOSPHATASE (ACP) i useful for evaluation of _____________________

A

metastatic-prostatic carcinoma

354
Q

ACID PHOSPHATASE

TOTAL ACP
RR: Male

A

2-5-11.7 U/L

355
Q

ACID PHOSPHATASE

PROSTATIC ACP
RR: Male

A

0.2-5.0 U/L

356
Q

ACID PHOSPHATASE

TOTAL ACP
RR: Female

A

0.3-9.2 U/L

357
Q

ACID PHOSPHATASE

PROSTATIC ACP
RR: Female

A

0.0-0.8 U/L

358
Q

T/F: Total ACP is measured in the laboratory

A

True

359
Q

Method of Analysis (ACP)

Specimen

A

Serum

360
Q

Method of Analysis ACP

Substrates

A

Thymolphthalein monophosphate
α-naphthyl phosphate

361
Q

Substrate to use in ACP for end-point methods

A

Thymolphthalein monophosphate

362
Q

Specific substrate for prostatic ACP

A

Thymolphthalein monophosphate

363
Q

ACP substrate for continuous monitoring methods/kinetic assay

A

α-naphthyl phosphate

364
Q

Methods of Analysis ACP

INHIBITORS

A

L-Tartrate
2% formaldehyde, cupric sulfate solution

365
Q

Inhibitor in ACP that inhibits prostatic ACP

A

L-Tartrate

366
Q

Inhibitor in ACP that also Inhibit lysosomal ACP

A

L-Tartrate

367
Q

Inhibitor in ACP that inhibits RBC ACP/TRAP

A

2% formaldehyde, cupric sulfate solution

368
Q

Method of Analysis ACP

Storage

A

Frozen
Acidified

369
Q

ACP is acidified in what pH

A

< pH of 6.5

370
Q

When ACP is acidified, ACP is stable for ______ @ ________

A

2 days
Room temp

371
Q

Methods of Analysis ACP

Variables

A

Room temp
Bilirubin
Hemolysis
Heparin, Oxalate, Fluorides

372
Q

VARIABLES (ACP)

Room temp
-ACP stable within ________ @ RT because CO2 from
blood sample is released which (increases/decreases) pH of the sample

A

1-2 hrs
increases

373
Q

false (decrease/increase) due TRAP/RBC ACP

A

Bilirubin - decrease
Hemolysis - increase

374
Q

Heparin, Oxalate, Fluorides -
false (decrease/increase)

A

decrease

375
Q

in measuring prostatic ALP what is the inhibitor

A

(L. tartrate -

376
Q

Enumerate the steps in measurign prostatic ACP

A
  1. Measure total ACP
  2. Add L-tartrate
  3. Measure total ACP (TRAP)
    ○ Prostatic ACP = Total ACP - TR
377
Q

Enumerate the different kind of ACP methods

A
  1. Gutman and Gutan
  2. Shinowara
  3. Babson, Read & Philips
  4. Roy and Hillman
378
Q

GUTMAN AND GUTAN

Substrate

A

Phenyl phosphate

379
Q

GUTMAN AND GUTAN

End product

A

Inorganic phosphate

380
Q

SHINOWARA

Substrate

A

P-nitrophenylphosphate

381
Q

SHINOWARA

End Product

A

p-nitrophenol

382
Q

Babson, Read & Philips

Substrate

A

α-naphthylphosphate

383
Q

BABSON, READ & PHILIPS

End product

A

α-naphthol

384
Q

ROY AND HILLMAN

Substrate

A

Thymolphthalein monophosphate

385
Q

ROY AND HILLMAN

End product

A

Free thymolphthalein

[LAB] CC2 (2 decks)

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