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CC II (lec) > Clinical Enzymology Part 2 > Flashcards

Clinical Enzymology Part 2 Flashcards

1
Q

What are the 2 pancreatic enzymes

A

Amylase
Lipase

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2
Q

Amylase is also known as?

A

a-1,4-glucan-4-glucohydrolase

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3
Q

It is the smallest enzyme which can be freely filtered by the glomerulus

A

amylase

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4
Q

T/F

Amylase is NOT normally present in urine

A

F; it is normally present in urine

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5
Q

The earliest pancreatic marker

A

Amylase

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6
Q

Amylase

Rise:
Peak:
Normalize:

A

Rise: 5-8 hrs,
Peak: 24 hrs
Normalize: 3-5 days

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7
Q

The rise, peak and normalization of amylase should be accompanied by (increase, decrease) urine amylase, which usually elevated within ______ upon onset of _________

A

increase
7 days
acute pancreatitis

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8
Q

Catalyzes the hydrolysis of 1,4-glycosidic bonds in polysaccharides

A

Amylase

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9
Q

Amylase catalyzes the hydrolysis of what bond in polysaccharides?

A

1,4-glycosidic bonds

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10
Q

Example of polysaccharides

A

starch, glycogen

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11
Q

Refers to long chains of glucose molecules

A

polysaccharides

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12
Q

Once starch and glycogen are hydrolyzed, the product is________

A

glucose

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13
Q

2 activators of Amylase

A

Calcium, Chloride

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14
Q

Major Tissue Sources of amylase

A

-Pancreas (Acinar Cells) and Salivary Glands

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15
Q

Other tissue sources of amylase

A

-Adipose Tissues, Fallopian Tubes, Small Intestines, Skeletal Muscles

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16
Q

Reference range of amylase
Serum: ______
Urine: _______

A

Serum: 28-100 U/L
Urine: 1-15 U/h

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17
Q

TYPES OF GLYCOSIDIC BONDS

A

α-glycosidic bond
β-glycosidic bond

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18
Q

T/F:
α-glycosidic bond is oriented down

A

T

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19
Q

T/F
β-glycosidic bond is oriented up

A

T

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20
Q

has branches (α-1,6-glycosidic bond)

A

Amylose

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21
Q

2 types of Isoenzymes

A

S-type isoamylase
P-type isoamylase

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22
Q

S-type isoamylase is aka

A

Ptyalin or Salivary Amylase

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23
Q

Initiate hydrolysis of polysaccharides in the mouth

A

S-type isoamylase

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24
Q

Example/group of S-type isoamylase

A

S1, S2, S3

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25
Q

The most anodal AMY isoenzyme

A

S-type isoamylase

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26
Q

P-type isoamylase is aka

A

aka Pancreatic Amylase and Amylopsin

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27
Q

Increased isoenzymes in acute pancreatitis

A

P-type isoamylase

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28
Q

Example/group of P-type isoamylase

A

P1, P2, P3

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29
Q

the most predominant pancreatic amylase isoenzyme in acute pancreatitis.

A

P3

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30
Q

Increased amylase is aka

A

Hyperamylasemia

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31
Q

What are the 8 diseases/condition associated with increased amylase (Hyperamylasemia)

A

Acute Pancreatitis
Parotitis
Perforated Peptic Ulcer
Intestinal Obstruction
Cholecystitis
Ruptured Ectopic Pregnancy
Mesenteric Infarction
Acute Appendicitis

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32
Q

The specimen used in Amylase

A

Serum, Heparinized Plasma

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33
Q

The substrate used in AMY

A

Starch

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34
Q

In all methods of analysis for Amylase, we measure the ____

A

Total Amylase

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35
Q

T/F
In all methods of analysis for Amylase, we measure the Total Amylase. Hence, we S-type and P-type should be classified

A

F; we don’t classify S-type and P-type.

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36
Q

What are the 4 methods of analysis in amylase

A

Saccharogenic
Amyloclastic
Chromogenic
Couple-Enzyme

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37
Q

Classical method (AMY)

A

Saccharogenic

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38
Q

It measures the amount of reducing sugars produced by the hydrolysis of starch by the usual glucose method

A

Saccharogenic

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39
Q

Saccharogenic measures the amount of _________ produced by the ________ of starch by the usual glucose method

A

reducing sugars
hydrolysis

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40
Q

It measures decrease in starch substrate

A

Amyloclastic

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41
Q

Substrate in Amyloclastic are coupled with ______ and will yield what color

A

iodine
Starch + Iodine = Bluish Black Color

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42
Q

Decrease in color is proportional to AMS activity

A

Amyloclastic

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43
Q

In amyloclastic, the ______ (less, more) color of the substrate, the ____ (less, more) enzyme activity in the solution

A

less
more

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44
Q

Measures the formation of Soluble Starch Fragments coupled with chromogenic dyes.

A

Chromogenic

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45
Q

Color intensity is proportional to AMS activity

A

Chromogenic

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46
Q

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

A

Couple-Enzyme

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47
Q

The substrate used in couple-enzyme (Method of Analysis in Amylase)

A

Starch

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48
Q

The wavelength used in couple-enzyme (Method of Analysis in Amylase)

A

340 nm

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49
Q

pH level in couple-enzyme (Method of Analysis in Amylase)

A

6.9

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50
Q

Storage condition in couple-enzyme (Method of Analysis in Amylase)

A

Room temp (1 week), 4°C (2 months)

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51
Q

can be used to measure S-type and P-type isoenzyme.

A

Wheat Germ Lectin

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52
Q

Wheat Germ Lectin inhibits ____

A

Salivary Amylase

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53
Q

Steps in measuring S-type and P-type isoenzyme

A
  1. Measure Total Amylase
  2. Add Wheat Germ Lectin
  3. Measure Amylase (P-Type)
    SA = Total Amylase – Pancreatic Amylase
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54
Q

false decrease variables in AMY

A

-Ca2+ Chelating Anticoagulant (EDTA)
-Triglycerides

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55
Q

Why is Ca2+ Chelating Anticoagulant (EDTA) false decrease in AMY

A

Bec. Calcium is used as an activator for Amylase

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56
Q

false increase variables in AMY

A

Morphine, other opiates

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57
Q

Acute Pancreatitis + Hyperlipidemia = _____ (high, normal, low) Levels in Amylase

A

Normal

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58
Q

Amylase bound to immunoglobulin

A

Macroamylasemia

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59
Q

it is a type of Amylasemia that is Asymptomatic and it is not filtered by the glomerulus.

A

Macroamylasemia

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60
Q

_____ and ______ are measured to differentiate Macroamylasemia from Hyperamylasemia,

A

Serum and Urine amylase

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61
Q

Macroamylasemia = (increased, decreased) urine amylase

A

decreased

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62
Q

Hyperamylasemia = (inc., dec.,) serum and urine amylase

A

increased

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63
Q

Amylase/Creatinine Ratio:
Normal: ________
Acute Pancreatitis: ______

A

Normal: 1-4% (0.01-0.04)
Acute Pancreatitis: >4%-15%

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64
Q

What is the E.C. numerical code of Lipase

A

E.C. 3.1.1.3

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65
Q

Lipase is aka

A

Triacylglycerol Acylhydrolase

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66
Q

AKA Triacylglycerol Acylhydrolase

A

Lipase

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67
Q

Catalyzes hydrolysis of glycerol esters of complex lipids to produce alcohol and fatty acid.

A

Lipase

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68
Q

Catalyzes partial hydrolysis of dietary TAG to 2-monoglyceride intermediate, with production of long-chain fatty acids.

A

Lipase

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69
Q

Cofactors of lipase

A

Colipase (coenzyme), Bile salts

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70
Q

Major Tissue Source of lipase

A

Pancreas

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71
Q

Other Tissue Source of lipase

A

Stomach, Small Intestines

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72
Q

Reference Range of lipase

A

<38 U/L

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73
Q

The MOST specific pancreatic marker

A

lipase

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74
Q

In chronic pancreatitis: (lipase)

  • ______ are destroyed
  • Loss of ____ and _____
A

Acinar cells
AMS, LPS

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75
Q

RISE:

AMS: ____
LPS: _____

A

5-8 hrs

4-8 hrs

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76
Q

PEAK:

AMS: ___
LPS: ____

A

both: 24 hrs

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77
Q

NORMALIZE:

AMS: ____
LPS: ____

A

3-5 days

8-14days

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78
Q

the specimen used in the methods of analysis of lipase

A

Serum

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79
Q

the storage condition used in the methods of analysis of lipase

A

room temp (1 week), 4°C (3 weeks)

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80
Q

interferences in the methods of analysis of lipase

A

hemolysis

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81
Q

hemolysis causes false ____ (inc., dec.,) n Lipase activity because hemoglobin interferes with lipase

A

decrease

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82
Q

3 methods used in the analysis of lipase

A

Cherry-Crandall Method
Tietz and Fierech
Peroxidase Coupling

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83
Q

Reference method in LPS

A

Cherry-Crandall Method

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84
Q

The substrate in Cherry-Crandall Method of LPS

A

50% Olive Oil

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85
Q

The end product in Cherry-Crandall Method of LPS

A

Fatty Acids (titrated and measured)

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86
Q

What method of LPS has this principle: Hydrolysis of olive oil for 24 hours producing fatty acids which are titrated

A

Cherry-Crandall Method

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87
Q

Most commonly used method in LPS

A

Peroxidase Coupling

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88
Q

Does NOT use 50% olive oil

A

Peroxidase Coupling

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89
Q

What are the 2 cardiac enzymes

A

Creatine kinase
Lactate dehydrogenase

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90
Q

Creatinine kinase is aka

A

ATP Creatine-N-Phosphotransferase

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91
Q

Catalyzes phosphorylation of creatine to form creatine phosphate.

A

CREATINE KINASE

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92
Q

Involved in storage of high-energy creatine phosphate in the muscles.

A

Creatine kinase

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93
Q

T/F:

Creatine kinase is a dimeric molecule

A

T

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94
Q

What are the dimeric molecules in creatine kinase

A

M subunit
B subunit

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95
Q

M subunit refers to

A

muscle

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96
Q

B subunit refers to

A

brain

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97
Q

Major Tissue Source of creatine kinase

A

brain, muscles (smooth, skeletal, cardiac)

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98
Q

Reference ranges (Creatine kinase)

Male: _____
Female: _____
CK-MB: ___

A

Male: 46-171 U/L
Female: 35-145 U/L
CK-MB: <5% of total CK

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99
Q

T/F:
Male has higher muscle mass than females

A

T

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100
Q

What are the normal isoenzymes

A

CK-BB
CK-MB
CK-MM

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101
Q

What isoenzyme is CK-1

A

CK-BB

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102
Q

What isoenzyme is CK-2

A

CK-MB

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103
Q

What isoenzyme is CK-3

A

CK-MM

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104
Q

Most anodal CK

A

CK-BB

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105
Q

2nd most anodal CK

A

CK-MB

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106
Q

3rd most anodal CK

A

CK-MM

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107
Q

Brain type isoenzyme

A

CK-BB

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108
Q

Hybrid type isoenzyme

A

CK-MB

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109
Q

Muscle type isoenzyme

A

CK-MM

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110
Q

Dominant in brain, intestines, and smooth muscles

A

CK-BB

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111
Q

Present in significant concentration in the cardiac muscles

A

CK-MB

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112
Q

Abundantly present in striated muscles

A

CK-MM

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113
Q

CK-BB is Rarely found in ____

A

serum (it cannot pass through the blood-brain barrier))

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114
Q

Serodiagnostic tool for AMI (Acute Myocardial Infarction)

A

CK-MB

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115
Q

Major Isoenzyme in normal individual (94-100%)

A

CK-MM

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116
Q

Useful Non-Specific Tumor Marker

A

CK-BB

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117
Q

Reference value OF CK-MB

A

<5% of Total CK

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118
Q

Myocardial Damage/AMI of CK-MB
-____ (elevated, decreased) CK-MB
- ____ of Total CK

A

Elevated
≥ 6

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119
Q

2 abnormal isoenzymes

A
  • MACRO-CK
  • Mitochondrial CK
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120
Q

In MACRO-CK:

CK-BB + ______
CK-MM + ________

A

Immunoglobulin
Lipoproteins

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121
Q

T/F

MACRO-CK is associated with any disease

A

F; not associated

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122
Q

It requires intensive tissue damage for it to be present

A

Mitochondrial CK

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123
Q

T/F:

in serum, mitochondrial CK is NOT associated with any disease or disorder but it may be used as an indicator/marker of severe illness.

A

T

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124
Q

Conditions with an increased CK

A

Acute Myocardial Infarction
Duchenne-type Muscular Dystrophy
Rhabdomyolysis
Cerebrovascular Accident
Seizures
Nerve Degeneration
CNS Shock
Hypothyroidism
Malignant Hyperpyrexia
Reye’s Syndrome

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125
Q

CK-MB during Acute Myocardial Infarction

RISE: _____
PEAK: ____
NORMALIZE: ____

A

Rise: 4-8 hrs.
Peak: 12-24 hrs.
Normalize: 48-72 hours

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126
Q

it shows the highest elevation of total creatine kinase

A

Duchenne-type Muscular Dystrophy

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127
Q

T/F:

Stress in muscle tissues results to increase CK

A

T

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128
Q

Conditions/activity that causes stress in muscle tissues resulting to increase CK

A

Crush syndrome, tetany, surgical incisions
Strenuous exercise, contact sports
IM Injection

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129
Q

Early diagnostic tool for Vibrio vulnificus infection

A

Creatine Kinase

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130
Q

flesh-eating bacterium

A

Vibrio vulnificus

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131
Q

causes Necrotizing fasciitis

A

Vibrio vulnificus

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132
Q

measures the creatinine kinase progesterone ratio

A

ectopic pregnancies

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133
Q

2 methods of analysis in CK

A

-Tanzer-Gilbard Assay
-Oliver-Rosalki Method

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134
Q

Forward/Direct Method

A

Tanzer-Gilbard Assay

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135
Q

Tanzer-Gilbard Assay:

coupled with: _____, _____, _____

A

Pyruvate Kinase, Lactate Dehydrogenase, and ADH System

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136
Q

Optimal pH in Tanzer-Gilbard Assay

A

9.0 (alkaline/basic)

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137
Q

Wavelength in Tanzer-Gilbard Assay

A

340 nm

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138
Q

Reverse/Indirect Method

A

Oliver-Rosalki Method

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139
Q

Most commonly performed method

A

Oliver-Rosalki Method

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140
Q

Why is Oliver-Rosalki Method
most commonly performed method

A

bec. it is 2-6x faster the Tanzer-Gilbard Assay

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141
Q

Oliver-Rosalki Method:

coupled with: ___

A

Hexokinase-Glucose-6-Phosphate -Dehydrogenase-NADP System

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142
Q

Optimal ph in Oliver-Rosalki Method

A

6.8 (Slightly Acidic)

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143
Q

wavelength in Oliver-Rosalki Method

A

340 nm

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144
Q

specimen used in Oliver-Rosalki Method

A

Serum, Heparinized Plasma

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145
Q

inhibitor of sulfhydryl group oxidation.

A

N-acetylcysteine, mercaptoethanol, thioglycerol, dithiothreitol

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146
Q

3 variables in Oliver-Rosalki method

A

-hemolysis
-light
-non-heparinized anticoagulant

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147
Q

Variables (Oliver-Rusalki method)

Hemolysis ( ____HGB)

A

> 320 mg/L

148
Q

T/F:
Oliver-Rosalki Method:

In the presence of hemolysis, CK is falsely elevated even CK is not found in RBC

A

T

149
Q

causes false elevation of CK activity

A

Adenylate Kinase

150
Q

Added to inhibit/inactivate Adenylate Kinase

A

Adenosine Monophosphate

151
Q

Added to inhibit/inactivate Adenylate Kinase

A

Adenosine Monophosphate

152
Q

T/F:

CK is inactivated by light

A

T

153
Q

What are the 4 methods of isoenzyme analysis

A

-Electrophoresis
-Ion-Exchange Chromatography
-Antibody-Inhibition
-Immunoassays

154
Q

Reference method of isoenzyme analysis (CK)

A

Electrophoresis

155
Q

In electrophoresis, Macro CK migrates between _____ and _____

A

CK-MM and CK-MB

156
Q

It is potentially MORE sensitive and precise than electrophoresis

A

Ion-Exchange Chromatography

157
Q

Errors in Ion-Exchange Chromatography

A

-CK-MM merge with CK-MB
-CK-BB eluted with CK-MB
-Macro-CK eluted with CK-MB

158
Q

Used Anti-M antibodies

A

Antibody-Inhibition

159
Q

Antibody-inhibition can detect ____ activity if present resulting to falsely ______ CK-MB activity

A

CKBB
elevated

160
Q

a more specific method for CK-MB

A

Double-Antibody Immunoinhibition

161
Q

It measures the enzyme protein rather than the activity of the enzyme. We can measure even the inactivated enzyme because we measure the CONCENTRATION.

A

Immunoassays

162
Q

Catalyzes the oxidation of lactic acid to pyruvic acid with mediation of NAD+ as the hydrogen acceptor.

A

Lactate dehydrogenase

163
Q

T/F:

The catalytic activity of LACTATE DEHYDROGENASE is IRREVERSIBLE.

A

F; reversible

164
Q

It is present virtually in all cells of the body.

A

LACTATE DEHYDROGENASE

165
Q

Coenzyme of LD

A

Oxidized NAD+

166
Q

Inhibitor of LD

A

EDTA

167
Q

contain H or M Unit/Peptide

A

Tetrametic Molecule

168
Q

Tissue sources of Lactate Dehydrogenase

A

heart, RBCs, kidneys, lungs, pancreas, spleen, skeletal muscles, liver, intestines

169
Q

Reference value of LD

A

125-220 U/L

170
Q

What are the Lactate dehydrogenase isoenzymes

A

LD1
LD2
LD3
LD4
LD5
LD6

171
Q

LD1 subunits

A

HHHH

172
Q

LD1 Tissue source

A

Heart, RBC

173
Q

LD1 % based on total LDH

A

14-26

174
Q

Most predominant isoenzyme in LD

A

LD2

175
Q

LD2 subunits

A

HHHM

176
Q

LD2 tissue source

A

Heart, RBC

177
Q

LD2 % based on total LDH

A

29-39%

178
Q

increased in pulmonary involvement and various carcinomas

A

LD3

179
Q

LD3 subunits

A

HHMM

180
Q

LD 3 tissue source

A

Liver, Spleen, Lymphocytes, Pancreas

181
Q

LD 3 based on total LDH

A

20-26%

182
Q

LD 4 subunits

A

HMMM

183
Q

LD 4 tissue source

A

Liver

184
Q

LD 4 % based on Total LDH

A

8-16%

185
Q

LD 5 is seen in ___

A

muscular injuries

186
Q

LD 5 subunits

A

MMMM

187
Q

LD 5 tissue source

A

Skeletal muscle

188
Q

LD6 is aka

A

alcohol dehydrogenase

189
Q

LD 6 is present in _____

A

Arteriosclerotic cardiovascular failure

190
Q

Most predominant to leasT predominant LD (normal path)

A

LD 2>1>3>4>5

191
Q

used as tumor markers for Acute Leukemia, Germ Cell Tumor, Breast Cancer, and Lung Cancer.

A

LD 2, 3 & 4

192
Q

T/F:

Increase in Total LDH is SIGNIFICANT.

A

F; INSIGNIFICANT

193
Q

Increased LDH is seen in:

A

-Acute Myocardial Infarction
-Hemolytic anemia
-Pernicious anemia
-Pulmonary infarction
-Muscle dystrophy
-Hepatic carcinoma, toxic hepatitis, cirrhosis, viral hepatitis
-Blood transfusion
-Pneumocystis jirovecii infection

194
Q

Increased LDH:

Acute Myocardial Infarction
Rise: ___
Peak: ___
Normalize: ___
Exhibits LDH Flipped Pattern: ____

A

Rise: 12-24 hrs
Peak: 48-72 hrs.
Normalize: After 10-14 days
Exhibits LDH Flipped Pattern: LD1 > 2 > 3 > 4 > 5

195
Q

Increased LDH:

Hemolytic anemia
Exhibits LDH Flipped Pattern: ___

A

LD1 > 2 > 3 > 4 > 5

196
Q

Increased LDH:

Pernicious anemia
Exhibits LDH Flipped Pattern: ___

A

LD1 > 2 > 3 > 4 > 5

197
Q

Increased LDH:

Pulmonary infarction
Pattern: ___

A

LD 3 > 4 > 2 > 1 > 5

198
Q

Increased LDH:

Muscle dystrophy
Pattern: ___

A

LD 5 > 4 > 3 > 2 > 1

199
Q

May cause an increase in Lactate Dehydrogenase but it will NORMALIZE within 24 hrs. after the blood transfusion.

A

Blood transfusion

200
Q

Specimen in LDH

A

Serum

201
Q

Substrate used in LDH

A

Lactate (Most commonly used),
Pyruvate of α-hydroxybutyrate (Specific to LD1)

202
Q

Most common substrate used in LDH

A

Lactate

203
Q

Storage (LDH)

Total LD: _____
LD Isoenzymes: _____

A

25°C (48 hours)
25°C (24 hours)

204
Q

Variables in LDH method of analysis

A

-plasma specimen
-hemolysis
-cold storage

205
Q

In LDH, plasma specimen causes _______ because of presence of platelets in plasma

A

false increase

206
Q

The presence of hemolysis in LDH can cause ____ of LD because RBC has ____ more Lactate dehydrogenase than serum (specifically____ and _____)

A

false elevation
100-150x
LD1 & LD2

207
Q

Cold storage in LDH:

old, and labile causes a false ____ (specifically ___ and ___)

A

decrease
LD4 & LD5

208
Q

2 methods in Lactate dehydrogenase

A

Wacker Method
Wrobleuski La Due

209
Q

Forward/Direct Method in LDH

A

Wacker Method

210
Q

Most commonly used method in LDH

A

Wacker Method

211
Q

Wacker Method:

pH: ___
Wavelength: ___

A

pH: 8.3-8.9
Wavelength: 340 nm

212
Q

Reverse/Indirect Method of LDH

A

Wrobleuski La Due

213
Q

T/F
Wrobleuski La Due is thrice the rate of forward method

A

T

214
Q

Wrobleuski La Due is the preferred method for

A

Dry-Slide Technology

215
Q

Example of Dry-Slide Technology

A

Vitros

216
Q

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

A

Wrobleuski La Due

217
Q

pH of Wrobleuski La Due

A

7.1-7.4

218
Q

2 NON ENZYMATIC CARDIAC MARKERS

A

Myoglobin
Cardiac troponins

219
Q

The primary oxygen-carrying protein found in striated skeletal and cardiac muscle.

A

Myoglobin

220
Q

Screening test for myocardial infarction

A

Myoglobin

221
Q

The earliest marker for MI

A

myoglobin

222
Q

MYOGLOBIN:

Rise: ___
Peak: ___
Normalize: ____

A

Rise: 1-3 hrs
Peak: 5-12 hrs
Normalize: 18-30 hrs (ave. 24 hrs.)

223
Q

Gold standard in diagnosis of AMI

A

. Cardiac Troponins

224
Q

A complex protein that resides in the filaments of cardiac (____) and skeletal muscle (___)

A

Cardiac Troponins
94-97%
3-6%

225
Q

Regulators of actin and myosin

A

Cardiac Troponins

226
Q

responsible for muscle contraction

A

actin and myosin

227
Q

3 subunits of cardiac troponins

A

Troponin T
Troponin I
Troponin C

228
Q

Tropomyosin-binding subunit

A

Troponin T

229
Q

Sensitive marker for diagnosis of unstable angina

A

Troponin T

230
Q

In troponin T, a value of _____ is suggestive of AMI

A

≥ 1.5 ng/mL

231
Q

Absent from normal serum

A

Troponin T

232
Q

2 subunits of cardiac troponins that are NOT cardiac specific

A

Troponins T & C

233
Q

Inhibitory subunit

A

Troponin I

234
Q

Cardiac-specific and sensitive

A

Troponin I

235
Q

Troponin I is only found in ___

A

Myocardium

236
Q

Absent from normal serum

A

Troponin I

237
Q

Calcium-binding subunit

A

Troponin C

238
Q

Regulates muscle contraction

A

Troponin C

239
Q

Troponin T

Rise: ___
Peak: ____
Normalize: ___

A

3-4 hrs
10-24 hrs
7 days

240
Q

Troponin I:

Rise: ___
Peak: ____
Normalize: ___

A

3-6 hrs
12-18 hrs
5-10 days

241
Q

Acute Myocardial Infarction: (T/F)

Aspartate aminotransferase is NOT liver-specific

A

T

242
Q

Aspartate aminotransferase:

Rise: __
Peak: ___
Normalize: ___

A

6-8 hrs
24 hrs
Within 5 days

243
Q

T/F:

Creatine Kinase-MB is cardiac specific

A

T

244
Q

Creatine Kinase-MB:

Rise: __
Peak: ___
Normalize: ___

A

4-8 hrs
12-24 hrs
48-72 hrs

245
Q

Lactate Dehydrogenase:

Rise: __
Peak: ___
Normalize: ___

A

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

246
Q

Myoglobin:

Rise: __
Peak: ___
Normalize: ___

A

1-3 hrs
5-12 hrs
18-30 hrs (ave. 24)

247
Q

Troponin T:

Rise: __
Peak: ___
Normalize: ___

A

3-4 hrs
10-24 hrs
7 days

248
Q

Troponin I:

Rise: __
Peak: ___
Normalize: ___

A

3-6 hrs
12-18 hrs
5-10 days

249
Q

OTHER CLINICALLY SIGNIFICANT ENZYMES

A

Acid phosphatase
Aldolase
Cholinesterase
Angiotensin-Converting Enzyme
Glucose-6-Phosphate Dehydrogenase
Ceruloplasmin

250
Q

ACID PHOSPHATASE is aka

A

Acid orthophosphoric monoester phosphohydrolase

251
Q

aka. Acid orthophosphoric monoester phosphohydrolase

A

ACID PHOSPHATASE

252
Q

Catalyzes the same reaction as ALP but at pH 5.0 (Optimum pH)

A

ACID PHOSPHATASE

253
Q

Major Tissue Source of Acid Phosphatase

A

Prostate

254
Q

Other Sources of acid phosphatase

A

Erythrocytes, platelets, liver, bone, spleen, kidneys.

255
Q

Reference ranges for total ACP:

Male: ___
Female: ___

A

2-5-11.7 U/L
0.3-9.2 U/L

256
Q

Reference ranges for Prostatic ACP:

Male: ___
Female: ___

A

0.2-5.0 U/L
0.0-0.8 U/L

257
Q

For detection of prostatic carcinoma (metastatic carcinoma)

A

ACID PHOSPHATASE

258
Q

found in hairy cell leukemia

A

Tartrate-Resistant ACP (TRAP)

259
Q

Tartrate-Resistant ACP (TRAP) is aka

A

Erythrocyte Acid Phosphatase

260
Q

Tartrate-Resistant ACP (TRAP) is a marker for:
______ & ____

A

Marker for Bone remodeling
Marker for Metastatic Cancer in Bone Marrow

261
Q

t/f:
Post-Prostatectomy is under the diagnostic significance of ACP

A

T

262
Q

T/F: (ACP)

Thrombocytopenia - Increased ACP because of increased platelet destruction

A

T

263
Q

T/F: (ACP)

Thrombocytopenia - Increased ACP because of increased platelet destruction

A

T

264
Q

T/F: (ACP)

Thrombocytopenia - Increased ACP because of increased platelet destruction

A

T

265
Q

Increased ACP (assoc. with bone disease):

A

Paget’s disease
Breast Cancer (with bone metastases)
Gaucher’s Disease (with bone marrow infiltration)

266
Q

Detection of Seminal Fluid-ACP activity

A

Rape cases

267
Q

Specimen used in rape cases (ACP)

A

Vaginal Washings (ACP in vaginal washing is stable for 4 days)

268
Q

Detectability of ACP in rape cases

A

4 days

269
Q

ACP Activity in rape cases

A

> 50 IU/L

270
Q

Specimen in ACP

A

serum

271
Q

Substrate in ACP

A

-Thymolphthalein monophosphate
-α-naphthyl phosphate

272
Q

end-point methods/fixed point method.

A

Thymolphthalein monophosphate

273
Q

specific substrate for prostatic ACP

A

Thymolphthalein monophosphate

274
Q

Continuous monitoring methods

A

α-naphthyl phosphate

275
Q

Inhibitors IN ACP

A

L-Tartrate

2% formaldehyde, cupric sulfate solution

276
Q

inhibits prostatic ACP and lysosomal ACP

A

L-Tartrate

277
Q

Not specific for prostatic ACP

A

L-Tartrate

278
Q

inhibits RBC/Erythrocyte ACP, aka TRAP

A

2% formaldehyde, cupric sulfate solution

279
Q

Storage in ACP

A

Frozen
Acidified

280
Q

Acified at a pH of____
ACP is stable for ____ at room temp.

A

<6.5
2 days

281
Q

Variables in ACP

A

-Room temp
-bilirubin
-hemolysis
-heparin, oxalate, fluoride

282
Q

T/F:

at room temp., ACP activity is decreased within 1-2 hours because CO2 from blood sample is released which increases pH of the sample

A

T

283
Q

T/F:

CO2 is not a principal acid component of the blood.

A

F; CO2 is one of the principal acid components of the blood.

284
Q

Bilirubin in ACP is falsely ____ (TRAP)

A

decreased

285
Q

Hemolysis in ACP is false ____ due to Erythrocyte ACP/TRAP

A

increased

286
Q

Heparin, Oxalate, Fluorides causes a false ___ in ACP

A

decreased

287
Q

To measure prostatic ACP, use inhibitors like ____

A

L-tartrate

288
Q

Measuring Prostatic ACP steps

A
  1. Measure Total ACP
  2. Use inhibitor (L-tartrate)
  3. Measure ACP – TRAP
    Prostatic ACP = Total ACP – TRAP
289
Q

ACP methods:

substrate in Gutman and Gutan:

A

Phenyl phosphate

290
Q

ACP methods:

end product in Gutman and Gutan:

A

Inorganic phosphate

291
Q

ACP methods:

substrate in Shinowara:

A

P-nitrophenylphosphate

292
Q

ACP methods:

end product in Shinowara:

A

p-nitrophenol

293
Q

ACP methods:

substrate in Babson, Read & Philips:

A

α-naphthylphosphate

294
Q

ACP methods:

end product in Babson, Read & Philips:

A

α-naphthol

295
Q

ACP methods:

substrate in Roy and Hillman:

A

Thymolphthalein monophosphate

296
Q

ACP methods:

endproduct in Roy and Hillman:

A

Free thymolphthalein

297
Q

With a numeral code of E.C. 4.1.2.13

A

ALDOLASE

298
Q

Aldolase is aka

A

Fructose-1,6-Diphosphate Aldolase

299
Q

Catalyzes the reversible reaction that splits fructose-1,6-diphosphate into two triose phosphate molecules

A

Aldolase

300
Q

Isoenzymes in Aldolase

A

Aldolase A
Aldolase B
Aldolase C

301
Q

FOR Skeletal muscles (Skeletal muscle marker)

A

Aldolase A

302
Q

For WBC, liver, kidney

A

Aldolase B

303
Q

For Brain tissues

A

Aldolase C:

304
Q

Increased Aldolase is seen in

A

Skeletal muscle disease, leukemia, hemolytic anemia, and hepatic cancers

305
Q

2 types of CHOLINESTERASE

A

Acetylcholinesterase
Pseudocholinesterase

306
Q

They are Anti-xenobiotic enzymes

A

CHOLINESTERASE

307
Q

CHOLINESTERASE is secreted by ___

A

liver (synthetic function)

308
Q

Catalyze the hydrolysis of the esters of choline

A

CHOLINESTERASE

309
Q

Catalyzes the removal of Benzyl Group of cocaine

A

CHOLINESTERASE

310
Q

Marker for Insecticide/Pesticide Poisoning (Organophosphate poisoning)

A

CHOLINESTERASE

311
Q

Used to monitor effects of muscle relaxants after surgery such as Succinylcholine

A

CHOLINESTERASE

312
Q

Involved in metabolism of anticholinergic drugs

A

CHOLINESTERASE

313
Q

They are INVERSE MARKERS for Acetylcholinerase

A

CHOLINESTERASE

314
Q

Methods for CHOLINESTERASE

A

Ellman technique and Potentiometry

315
Q

Variables in CHOLINESTERASE

A

Hemolysis

316
Q

Other names of Acetylcholinesterase

A

True Cholinesterase
Choline esterase I

317
Q

EC Numerical Codes of Acetylcholinesterase

A

E.C. 3.1.1.7

318
Q

Tissue source of Acetylcholinesterase

A

RBC, Lung, Spleen, Nerve endings

319
Q

Decreased in chronic exposure to organophosphates

A

Acetylcholinesterase

320
Q

Other names of Pseudocholinesterase

A

Choline Esterase II
Acylcholine acylhydrolase
Serum cholinesterase
Butyrylcholinesterase

321
Q

EC Numerical Codes of Pseudocholinesterase

A

E.C. 3.1.1.8

322
Q

Tissue source of Pseudocholinesterase

A

Liver, pancreas, heart, serum

323
Q

Decreased in acute toxicity with organophosphates

A

Pseudocholinesterase

324
Q

Decreased in hepatocellular diseases

A

Pseudocholinesterase

325
Q

RV of Pseudocholinesterase

Male:
Female:

A

Male: 4-78 u/L
Female: 33-76 U/L

326
Q

With an E.C numeral code of E.C. 3.4.15.1

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

327
Q

Kininase II, Peptidyl-Dipeptide A

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

328
Q

ANGIOTENSIN-CONVERTING ENZYME (ACE)is aka

A

Kininase II, Peptidyl-Dipeptide A

329
Q

T//F
ANGIOTENSIN-CONVERTING ENZYME (ACE) is a hydrolytic enzyme

A

T

330
Q

Converts angiotensin I to angiotensin II within the lungs (RAAS System)

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

331
Q

promotes sodium reabsorption

A

Aldosterone

332
Q

it will constrict the blood vessels, therefore, increasing the blood pressure of the patient.

A

Vasoconstriction

333
Q

It responds to hypertension

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

334
Q

T/F:

Angiotensin II Functions in decreasing Blood Pressure:

A

F; INCREASING

335
Q

ANGIOTENSIN-CONVERTING ENZYME (ACE)
Possible indicator of ____

A

Neuronal Dysfunction

336
Q

Target of blood pressure-lowering drugs (ACE inhibitors and Angiotensin II inhibitors)

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

337
Q

Tissue sources of ANGIOTENSIN-CONVERTING ENZYME (ACE)

A

lungs, testes, macrophage, epithelioid cells

338
Q

ANGIOTENSIN-CONVERTING ENZYME (ACE) is crucial for the diagnosis and monitoring of _____

A

sarcoidosis

339
Q

Increased ACE is seen in

A

Sarcoidosis, Multiple Sclerosis, Addison’s Disease
Acute/Chronic Bronchitis
HIV and Leprosy

340
Q

It maintains the NADPH in a reduced form to protect hemoglobin from oxidation and hemolysis.

A

GLUCOSE-6-PHOSPHATE DEHYDROGENASE (G6PD)

341
Q

Catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconate

A

GLUCOSE-6-PHOSPHATE DEHYDROGENASE (G6PD)

342
Q

GLUCOSE-6-PHOSPHATE DEHYDROGENASE (G6PD)
is involved in what pathway

A

Hexose Monophosphate Shunt

343
Q

Tissue sources of GLUCOSE-6-PHOSPHATE DEHYDROGENASE (G6PD)

A

Adrenal cortex, spleen, thymus, lymph nodes, lactating mammary gland, and erythrocytes.

344
Q

inherited X-linked trait common among African Americans

A

G-6-PD Deficiency

345
Q

G-6-PD Deficiency can lead to _______ after in-take of ______ which is an anti-malarial drug, and also after intake of _____

A

Drug-Induced Hemolytic Anemia
Primaquine
Favadins.

346
Q

It is detected in Newborn Screening

A

G-6-PD Deficiency

347
Q

RBC inclusion in G-6-PD Deficiency

A

Heinz bodies

348
Q

G-6-PD is increased during

A

Myocardial infarction, megaloblastic anemia

349
Q

RV for G-6-PD

A

7.9-16.3 U/g HGB

350
Q

Specimen (G6PD)

A

Red Cell Hemolysate - deficient
Serum - evaluate enzyme elevation

351
Q

A glycoprotein and a copper-binding enzyme

A

CERULOPLASMIN

352
Q

Imparts blue color to protein

A

CERULOPLASMIN

353
Q

Ceruloplasmin is a marker for

A

Wilson’s Disease

354
Q

Wilson’s Disease decreased Ceruloplasmin by ___

A

0.1 g/L

355
Q

Characterized by copper deposition in skin, liver, brain and cornea

A

CERULOPLASMIN

356
Q

Bluish-blue ring

A

Kayser-Fleisher Ring

357
Q

RV for ceruloplasmin

A

18-45 mg/dL

357
Q

RV for ceruloplasmin

A

18-45 mg/dL

358
Q

type of isoamylase that is excreted by salivary gland

A

S-type isoamylase

359
Q

type of isoamylase that is excreted by the pancreas

A

P-type isoamylase

360
Q

triacyglycerol is the other term for

A

triglycerides

361
Q

E.C numeral code for amylase

A

E.C. 3.2.1.1

362
Q

E.C. Numeral code for creatine kinase

A

E.C. 2.7.3.2

363
Q

E.C. Numeral code for lactate dehydrogenase

A

E.C. 1.1.1.27

364
Q

E.C. Numeral code for Acid phosphatase

A

E.C. 3.1.3.2

365
Q

LD 5 % based on Total LDH

A

6-16%

CC II (lec) (4 decks)

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