CLINICAL CHEMISTRY Flashcards

1
Q

Functions of Enzymes

A

1)Hydration of Carbon Dioxide (respiration)

2)Nerve induction

3)Muscle contraction

4)Nutrient degradation (digestion)

5)Growth and Reproduction

6)Energy storage and use

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2
Q

Aspartate Aminotransferase (AST)

A.K.A

A

Serum Glutamic Oxaloacetic Transaminase (SGOT)

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3
Q

enzyme not specific to the liver, widely distributed, highest activities in cardiac, liver, and skeletal muscles

A

AST

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4
Q

most abundant isoenzyme of AST

A

Cytoplasmic

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5
Q

Increased AST isoenzyme that indicates cell necrosis

A

Mitochondrial

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6
Q

AST reaction:

Aspartate + a-ketoglutarate ⇌

A

Oxaloacetate + Glutamate

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7
Q

After MI, AST begins to rise in

A

6-8 hours

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8
Q

AST level peaks at ____ after MI

A

24 hours

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9
Q

AST returns to normal state ___ after MI

A

5 days

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10
Q

AST is increased in

A

Hepatocellular and Skeletal muscle disease
Chronic disease of the liver with progressive damage

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11
Q

Cofactor tightly bound to an enzyme

A

Prosthetic group

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12
Q

Oxidized form of NAD measures:

A

decreased absorbance

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13
Q

Reduced form of NADH measures

A

Increase absorbance

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13
Q

Assay for AST that uses malate dehydrogenase and monitors absorbance at 340 nm

A

Karmen method

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14
Q

Reference range for AST

A

5-30 u/L

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15
Q

Hemolyzed samples in AST results

A

Falsely increase

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16
Q

Karmen Method:

Oxaloacetate + NADH+H ⇌ (MD) ⇌

end product

A

malate + NAD+ (oxidized form)

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17
Q

Serum glutamic-pyruvic transaminase (SGPT)

AKA

A

Alanine Aminotransferase (ALT)

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18
Q

Liver specific enzymes

A

ALT

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19
Q

Increased in acute inflammatory conditions of the liver

Used to monitor the course of hepatitis treatment and the effects of drug therapy

Screening post transfusion hepatitis

Screen blood donors

Markedly increased in jaundice

Used as test for occupational toxic exposure

A

ALT

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20
Q

ALT reaction:

Alanine + a-ketoglutarate ⇌

A

pyruvate + glutamate

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21
Q

shows the result of the AST and ALT measurements

A

De Ritis Ratio

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22
Q

De Ritis Ratio:

Ratio > 1

AST> ALT

A

Non-viral origin

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23
Q

De Ritis Ratio:

Ratio < 1

AST < ALT

A

Viral origin

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24
Q

Assay for ALT uses

A

Lactate dehydrogenase

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25
Q

Assay for ALT end product

Alanine + a-ketoglutarate ⇌ pyruvate + glutamate

Pyruvate + NADH + H ⇌

A

Lactate + NAD+

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26
Q

Methods to Detect AST and ALT

A

Reitman and Frankel

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27
Q

Major organ affected in AST/SGOT

A

Heart

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28
Q

Major organ affected in SGPT/ALT

A

Liver

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29
Q

Substrate for SGOT/AST

A

Aspartic alphaketoglutaric acid

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30
Q

Substrate for SGPT/ALT

A

Alanine Alphaketoglutaric acid

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31
Q

End products for SGOT/AST

A

Glutamic acid + Oxaloacetic acid

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32
Q

End products for SGPT/ALT

A

Pyruvic acid + glutamic acid

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33
Q

Color developer for SGPT and SGOT

A

2,4 DNPH

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34
Q

Color intensifier for ALT/AST

A

0.4 N NaOh

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35
Q

Used for the diagnosis of hepatobiliary disorders and chronic alcoholism, obstructive jaundice

A

GGT

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36
Q

GGT is located in the canaliculi of the hepatic cells specifically in

A

epithelial lining of the biliary ductules

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37
Q

Sensitive marker for ethanol intoxication, occult alcoholism

A

GGT

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38
Q

Glutathione + amino acid ⇌

End product

A

glutamyl-peptide + L-cysteinylglycine

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39
Q

Szaz assay for GGT:

absorbs ____ and is measured at 405-430 nm

A

p-nitroaniline

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40
Q

End product of Szas Assay:

y-glutamyl-p-nitroanilide + glycerine → GGTP →

A

y-glutamyl-glycylglycine + p-nitroaniline

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41
Q

Alkaline Phosphatase

AKA

A

Alkaline orthophosphoric monoester phosphohydrolase

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42
Q

Liberates inorganic phosphate from an organic phosphate ester with production of alcohol

A

Alkaline phosphatase

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43
Q

Reference range of ALP in adult

A

30-90 u/L (adult)

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44
Q

Reference range of ALP in 0-3 months

A

70-220 u/L

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45
Q

Reference range of ALP in 3-10 years

A

50-260 u/L

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46
Q

Reference range of ALP in 10 years to puberty age

A

60-295 u/L

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47
Q

Source of ALP

A

Liver, Bone (osteoblast), placenta, intestine, and renal tissues

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48
Q

In vivo activity of ALP requires — activator (example of cofactor that enhances enzyme activity by altering the spatial configuration of the active site of the enzyme for substrate finding)

A

Mg2+

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49
Q

Useful for hepatobiliary disease and bone marrow disorders

A

ALP

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50
Q

ALP is significantly increased in

A

Paget’s disease or Osteitis deformans

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51
Q

Predominant isoenzyme of ALP

A

Bone and Liver

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52
Q

Assay for ALP based on molar absorptivity of p-nitrophenol

pH of 10.2

A

Bowers and McComb

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53
Q

End product of Bowers and McComb ALP

p-Nitrophenyl-phosphate ⇌ ALP ⇌

A

p-nitrophenol + phosphate ion

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54
Q

Color result for Bowers and McComb

A

yellow (405 nm)

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55
Q

Substrate for Bodansky, Shinowara, Jones, Reinheart - ALP

A

B-glycerophosphate

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56
Q

Substrate for Bessy, Lowry and Brock

A

p-nitrophenyl phosphate

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57
Q

Bowers and McComb substrate

A

p-nitrophenyl phosphate

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58
Q

King and Armstrong substrate

A

Phenyl phosphate

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59
Q

End product for bodansky, shinowara, jones, reinhart

ACP

A

Inorganic PO4 + glycerol

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60
Q

End product for bessy, lowry, and brock

A

p-nitrophenol (yellow)

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61
Q

King and Armstrong end product

A

phenol

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62
Q

Electrophoresis for ALP

Most anodal to Least Anodal

A

Liver > Bone > Placental > Intestinal

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63
Q

Fastest isoenzyme of ALP in electrophoresis

A

Liver

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64
Q

Heat labile fraction of ALP

A

Bone

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65
Q

Bone ALP is increased in

A

bone disease
healing of bone fractures
physiologic bone growth

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66
Q

Most heat stable fraction in ALP

A

Placental

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67
Q

Physiologic increase of ALP

A

Increased in 16th or 28th week of pregnancy

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68
Q

Pathologic increase in placental ALP

A

Malignancy or cancer (carcinoplacental)

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69
Q

Placental ALP withstand heating at

A

65 degC for 30 mins

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70
Q

Slowest moving fraction in blood group B or O

A

Intestinal ALP

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71
Q

Increased in fatty meal consumption and GIT disorder (Isoenzyme)

A

Intestinal ALP

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72
Q

Placental and Intestinal ALP are inhibited by

A

phenylalanine

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73
Q

Inhibits Bone ALP

A

3M Urea

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74
Q

Inhibits bone and liver isoenzyme

A

Levamisole

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75
Q

Total ALP elevations by liver or Bone ALP is differentiated by heating of serum at

A

56 deg C for 10 minutes

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76
Q

Most stable to Most Labile in heat stability of ALP

A

Placental > Intestinal > Liver> Bone

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77
Q

ALP residual activity is ↓ to >20%

A

Liver ALP

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78
Q

ALP residual activity is ↓ to <20%

A

BONE ALP

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79
Q

Lung, Breast, and Gynecological cancers, bone ALP co-migrator, most heat stable ALP

Specific ALP that is most heat stable

A

REGAN ALP

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80
Q

Adenocarcinoma of the Pancreas and Bile duct, Pleural cancer

A

Nagao ALP

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81
Q

Inhibited by Phenylalanine reagent only

A

REGAN

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82
Q

Inhibited by both Phenylalanine and L-leucine. (Alp isoenzyme)

A

Nagao

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83
Q

Acid Phosphatase AKA

A

Acid Orthophosphoric Monoester phosphohydrolase

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84
Q

Phosphomonoester + H2O ⇌ ACP ⇌

End product

A

Alcohol + Phosphate ion

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85
Q

Catalyze the hydrolysis of various phosphomonoester at an acid pH

A

ACP

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86
Q

Liberate inorganic phosphate from an organic phosphate ester with production of alcohol

A

ACP

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87
Q

ACP is present in

A

Prostate, RBCs, Platelets, Bone (osteoclasts)

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88
Q

The activity of ACP in the seminal fluid is only demostrated for up to

A

4 days

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89
Q

inhibits specific prostatic ACP

A

L-tartrate ions

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90
Q

inhibits red cell ACP

A

Formaldehyde and Cupric ions

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91
Q

Reference Range: Prostatic ACP

A

0-3.5 ng/mL

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92
Q

Assay for ACP quantitative substrate

A

thymolpthalein monophosphate

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93
Q

Assay for ACP continuous substrate

A

a-napthyl phosphate

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94
Q

Assay for ACP gutman and gutman substrate

A

phenyl po4

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95
Q

Assay for ACP shinowara substrate

A

pnpp

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96
Q

Assay for ACP babson, read, and phillips substrate

A

alpha napthyl po4

97
Q

Assay for ACP roy and hillman substrate

A

thymolphthalein mono PO4

98
Q

End product of gutman and gutman

A

inorganic phosphate

99
Q

End product of shinowara

A

p-nitrophenol

100
Q

End product of babson, read, and phillips

ACP

A

alpha napthol

101
Q

End product of roy and hillman

A

free thymolphthalein

102
Q

Type of transferase enzyme that catalyze transfer of phosphate group between substrate

A

Creatine Kinase

103
Q

Creatine kinase is widely distributed and has highest activities in

A

skeletal muscle
heart (main source)
brain

104
Q

Creatine kinase end product:

creatine + atp ⇌ CK ⇌

A

creatine phosphate + ADP

105
Q

Creatine originates in the liver from

A

arginine
glycine
methionine

106
Q

Reference range of CK for Male

A

15-160 U/L

107
Q

Reference range of CK for female

A

15 to 130 U/L

108
Q

Forward reaction for CK

A

Tanzer-Gilvarg

109
Q

Primary enzyme in Tanzer Gilvarg

A

CK

110
Q

Tanzer Gilvarg reaction end product

A

Lactate + NAD

111
Q

Tanzer Gilvarg reaction:

Creatine + ATP ⇌CK⇌ Creatine phosphate + ADP

ADP + phosphoenolpyruvate ⇌ PK⇌ pyruvate + ATP

Pyruvate + NADH + H ⇌ LD⇌

A

Lactate + NAD

112
Q

Reverse Reaction for CK

A

Oliver Rosalki

113
Q

Increase absorbance at 340 nm for CK determination

A

Oliver Rosalki

114
Q

Decrease in absorbance at 340 nm for CK determination

A

Tanzer Gilvarg

115
Q

Secondary enzyme for Oliver Rosalki

A

HK and G6PD

116
Q

Secondary enzyme for Tanzer Gilvarg

A

PK and LD

117
Q

Hemolysis effect on CK

A

falsely increase

118
Q

Enzyme that has the same activity with CK

A

Adenelyte kinase

119
Q

inactivated by light (protect the tube from direct light exposure)

A

Creatine Kinase

120
Q

Physical activity and IM injections cause in CK

A

increase

121
Q

Bed ridden patients: CK activity is

A

decreased

122
Q

CK:

Slowest mobility toward the anode

Major isoenzyme in striated muscle and normal serum

A

CK-3/CK-MM/ Muscle type

123
Q

CK

Hybrid type (linked with acute myocardial infarction)

2nd fastest to migrate toward the anode

Significant quantities are found in heart tissues

A

CK-2/CK-MB

124
Q

CK

Migrate fastest towards the anode

Highest concentration in CNS, GI tract and uterus (pregnancy)

A large molecule that is not allowed to pass the blood brain barrier

A

CK-1/CK-BB/Brain type

125
Q

Healthy human serum CK-1 level

A

less than 1%

126
Q

After MI, CK-MB (>6%) levels begin to rise within

A

4-8 hours

127
Q

CK-MB peaks at _____ after MI

A

12-24 hours

128
Q

CK-MB returns to normal levels at

A

48-72 hours

129
Q

First enzyme to elevate during acute MI

A

CK-MB

130
Q

CK-MM reference value

A

94-98%

131
Q

CK-MB reference level

A

2-6%

132
Q

CK that complex with antibodies IgG/IgA

A

CK-BB

133
Q

CK complex with lipoproteins (Macro-CK)

A

CK-MM

134
Q

CK
Located midway between CK-MM and CK-MB

A

Macro-CK

135
Q

Increase level of indicates cell necrosis

Migrates cathodal to CK-MM

A

Mitochondrial CK-Mi

136
Q

Oxidoreductase enzyme that catalyzes interconversion of lactic and pyruvic acids

A

Lactate dehydrogenase

137
Q

Widely distributed, highest level activities in heart, hepatic, skeletal muscle and RBC

A

Lactate dehydrogenase

138
Q

Storage of the sample could affect the activity of LD

When the serum/plasma is frozen this could

A

decrease the activity of LD

139
Q

The activity of LD is maintained when the serum and plasma is stored at room temperature up to

A

2 days

140
Q

Assay for Lactate Dehydrogenase: forward reaction

A

Wacker Method

141
Q

LD assay:

Increase in absorbance is monitored at 340 nm
Optimal pH is ____

A

8.3-8.9

142
Q

Commonly used method for LD measurement

A

Wacker Method

143
Q

Wacker Method end product:

Lactate + NAD ⇌ LD ⇌

A

Pyruvate + NADH + H

144
Q

Reverse reaction for Lactate dehydrogenase

A

Wrobleuski La Due

145
Q

LD:

Decrease in absorbance is monitored at 340 nm

Three times faster but more susceptible to substrate exhaustion

A

Wrobleuski La Due

146
Q

Optimal pH for Wrobleuski La Due

A

7.1 to 7.4

147
Q

end product for wrobleuski la due

Pyruvate + NADH ⇌

A

Lactate + NAD

148
Q

Has greater affinity of H subunits

Can represent LDH-1 (the only isoenzyme that has 4H; HHHH)

A

a-hydroxybutyrate dehydrogenase

149
Q

a-hydroxybutyrate dehydrogenase end product:

a-ketobutyrate + NADH + H ⇌ a-HBD⇌

A

a-hydroxybutyrate

150
Q

after acute MI, LD begins to rise within

A

10 - 24 hours

151
Q

LD peaks at

A

48-72 hours

152
Q

LD remains elevated for

A

10 days

153
Q

Reference range of A-hydroxybutyrate dehydrogenase

A

100-225 u/L

154
Q

Markers for acute MI

A

CK-MB, Troponin I, CRP

155
Q

Last enzyme to persist in the serum of MI patient

can be used to monitor patients response to therapy

A

LDH

156
Q

LDH found in HEART AND RBC

A

LDF-1 (HHHH) and 2 (HHHM)

157
Q

LDH 1 is increased in

A

MI, Hemolytic anemia

158
Q

LDH 2 (HHHM) is increased in

A

RI, Megaloblastic anemia

159
Q

LDH 3 (HHMM) tissue source

A

Spleen, Pancreas, Lung

160
Q

LDH 4 (HMMM) tissue source

A

Liver

161
Q

LDH 5 (MMMM) tissue source

A

Skeletal muscle

162
Q

HHMM is increased in

A

pulmonary embolism

163
Q

HMMM is increased in

A

Hepatic injury

164
Q

MMMM is increased in

A

skeletal muscle injury

165
Q

LD concentration in healthy human serum

A

2, 1, 3, 4, 5
HHHM, HHHH, HHMM, HMMM, MMMM

166
Q

Acute MI and intravascular hemolysis concentration of LD

A

1,2,3,4,5 (FLIPPED PATTERN)

167
Q

LDH 6 is demonstrated in

A

Obstructive jaundice
Atherosclerotic failure
Hepatotoxicity

168
Q

↑ LDH-1 and ↑ CKMB results

A

possible AMI

169
Q

↑ LDH 1 and normal CKMB results

A

Hemolytic conditions

170
Q

CK MB appears —- after MI within

A

4-8 hours

171
Q

AST appears —- after MI

A

6-8 hours

172
Q

LDH appears within

A

10-24 hours

173
Q

CKMB peaks at

A

12-24 hours

174
Q

AST peaks at

A

24 hours

175
Q

LDH peaks at

A

48-72 hours

176
Q

CKMB stays elevated

A

3 days

177
Q

AST stays elevated for

A

5 days

178
Q

LDH stays elevated for

A

10 days

179
Q

Amylase and Lipase are released from the

A

acinar cells of the pancreas

180
Q

First enzyme to elevate in acute pancreatitis

A

Amylase

181
Q

Amylase breakdown starch and glycogen via

A

a,1-6 branching linkages

182
Q

Major tissue source of amylase

A

Pancreas, Salivary gland

183
Q

Minor tissue source of amylase:

A

adipose tissues, fallopian tubes, small intestine, skeletal muscles

184
Q

Amylase is increased in

A

acute pancreatitis, renal failure, and parotitis

185
Q

Amylase is ____ in cases of renal failure

A

increased

186
Q

amylase is increased after onset of acute pancreatitis in

A

2-12 hours

187
Q

Amylase peaks at

A

24 hours

188
Q

Amylase persists for

A

3-5 days

189
Q

Salivary Amylase
(fast moving) (more anodal)

A

ptyalin

190
Q

Pancreatic Amylase

A

amylopsin (slow moving)

191
Q

Assay for Amylase:

Measures the disappearance of starch substrate

A

Amyloclastic

192
Q

Amyloclastic:

Starch-Iodine Complex (Dark-blue) →

A

decrease in color intensity

193
Q

Amylase assay:

Measures the appearance of the product

A

Saccharogenic

194
Q

Saccharogenic assay:

Starch →

A

reducing sugars

195
Q

Assay for amylase:

directly proportional amylase activity with the reducing sugar

A

saccharogenic

196
Q

Amylase assay:

Activity of amylase is inversely proportional with the absorbance

A

Amyloclastic method

197
Q

Amylase methodologies:

measures the increasing color from production of product-chromogenic dye fragment

A

Chromogenic

198
Q

Insoluble starch dye →

Chromogenic end point:

A

soluble starch-dye fragment

199
Q

Coupling of several enzymes to monitor amylase activity

A

Continuous monitoring

200
Q

Endpoint of continuous monitoring for amylase:

A

5,6,-phosphogluconolactone + 5 NADH

201
Q

Secondary enzyme for amylase continuous monitoring

A

A-glucosidase, hexokinase, G6PD

202
Q

not excreted but is reabsorbed in plasma; amylase with antibodies

A

macroamylase

203
Q

Hydrolyzes the ester linkages of fats to produce alcohols and fatty acids

A

Lipase

204
Q

Specific to pancreatitis; early and specific marker for acute pancreatitis

A

Lipase

205
Q

Hydrolysis of dietary triglycerides in the intestine to 2-monoglyceride and fatty acids

A

Lipase

206
Q

Lipase increases after onset of acute pancreatitis in

A

6 hours

207
Q

Lipase peaks at

A

24 hours

208
Q

Lipase persists for

A

7 days

209
Q

Assay for Lipase:

Substrate for Cherry Crandall and Tietz

A

50% olive oil (triolein)

210
Q

Cherry Crandall and Tietz titrating agent

A

0.4N NaOH

211
Q

Indicator for Cherry Crandall

A

Phenolpthalein

212
Q

Indicator for Tietz

A

Thymolpthalein + Veronal

213
Q

End point for cherry crandall and tietz

A

fatty acid (oleic acid)

214
Q

End color cherry crandall

A

pink

215
Q

end color for tietz

A

blue

216
Q

Estimation of liberated fatty acids

A

Turbidimetric methods

217
Q

Measurement of the amount of light blocked by particles in soluble agents in the sample

A

Turbidimetric

218
Q

Reagent for turbidimetric methods

A

Triglyceride (hydrophobic; not polar, insoluble)

219
Q

Turbidimetric methods

Triacylglycerol + 2H2O ⇌

End product:

A

2-monoglyceride + 2 fatty acids

220
Q

A PHOSPHORIC MONOESTER HYDROLASE

Predominantly secreted in the liver
Marker for hepatobiliary disease

A

5’ NUCLEOTIDASE (5’N)

221
Q

Reference value for 5’ Nucleotidase (5’N)

A

0-1.6 UNITS

222
Q

INDEX OF PARENCHYMAL FUNCTION

USED TO MONITOR THE EFFECT OF MUSCLE

RELAXANTS (SUCCINYLCHOLINE) AFTER SURGERY

Secreted in the liver
Used as a marker for insecticide/pesticide poisoning (organophosphate)

A

CHOLINESTERASE/PSEUDOGHOLINESTERASE

223
Q

CHOLINESTERASE/PSEUDOGHOLINESTERASE REFERENCE VALUE:

A

0.5-1.3 UNITS (PLASMA)

224
Q

a.k.a PEPTIDYLDIPEPTIDASE A OR KININASE II

A

ANGIOTENSIN-CONVERTING ENZYME (ACE)

225
Q

Increased in angiotensin-converting enzyme (ACE)

A

Sarcoidosis, Acute and Chronic Bronchitis, and Leprosy

226
Q

Main source of angiotensin-converting enzyme

A

Macrophage And epithelioid cells (specifically in the lungs)

227
Q

important for vasoconstriction of the renal arterioles to increase blood pressure

Stimulates adrenal cortex to release aldosterone for reabsorption of sodium

A

Angiotensin II

228
Q

Used as a possible indicator of neuronal dysfunction

A

Angiotenstin Converting Enzyme

229
Q

Copper-Carrying protein which acts as an enzyme

A

Ceruloplasmin

230
Q

Ceruloplasmin is a marker for

A

Wilson’s disease

231
Q

Other enzyme marker for hepatobiliary diseases

A

Ornithine Carbamoyl Transferase (OCT)

232
Q

Ornithine Carbamoyl Transferase (OCT) reference values

A

8-20 mU/mL

233
Q

It functions to maintain NADPH in the reduced form in the erythrocytes

A

G6PD

234
Q

responsible for maintaining and stabilizing the membrane integrity of erythrocytes

A

Reduced NAD(PH)

235
Q

G6PD is found in

A

adrenal cortex
spleen
RBC
Lymph nodes

236
Q

G6PD Deficiency can lead to —- drug-induced hemolytic anemia

A

primaquine (antimalarial drug)

237
Q

Increased levels of G6PD

A

Myocardial infarction, megaloblastic anemia

238
Q

Specimen for G6PD

A

Red cell Hemolysate, Serum

239
Q

Reference values for G6PD

A

10 — 15 U/g Hgb or 1200 - 2000 mU/mL packed RBC