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CLINICAL CHEMISTRY > CC2 PRELIM (ENZYME, ABG, ELECTROLYTES TUMOR MARKERS) > Flashcards

CC2 PRELIM (ENZYME, ABG, ELECTROLYTES TUMOR MARKERS) Flashcards

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1
Q

are specific proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition.

A

Enzyme

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2
Q

A structure in which each enzyme contains a specific amino acid sequence

A

primary structure

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3
Q

A structure in which the resultant polypeptide chains adopting bends and turns

A

secondary structure

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4
Q

A structure in which an enzyme folding into a three-dimensional structure

A

tertiary structure

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5
Q

refers to the binding and interactions between the subunits.

A

quaternary structure

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6
Q

results when an enzyme is subject to posttranslational modifications with a functional group added to an amino acid.

A

isoform

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7
Q

it catalyzes an oxidation–reduction reaction between two substrates.

A

oxidoreductases

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8
Q

it catalyzes the transfer of a group other than hydrogen from one substrate to another.

A

Transferases

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9
Q

catalyze hydrolysis of various bonds.

A

hydrolases

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10
Q

catalyze the removal of groups from substrates without hydrolysis; the product contains
double bonds.

A

lyases

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11
Q

catalyze the interconversion of geometric, optical, or positional isomers.

A

isomerases

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12
Q

catalyze the joining of two substrate molecules, coupled with the breaking of the pyrophosphate bond in adenosine triphosphate (ATP) or a similar compound.

A

ligases

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13
Q

In EC number code, the 1st, 2nd, and 3rd number represent the

A

classification, subclass, and subsubclass

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14
Q

what classification is aldolase

A

lyases

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15
Q

ALP and ACP is what classification

A

hydrolases

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16
Q

AST, ALT, CK, and Pyruvate kinase is what classification

A

transferases

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17
Q

LD, G6PD, and Glutamate dehydrogenase is what classification

A

oxidoreductases

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18
Q

The excess energy needed to induce the transition state
is called

A

activation energy

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19
Q

it is based on the premise that the shape of the key (substrate) must fit into the lock (enzyme)

A

Emil Fisher’s/Lock and Key Theory

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20
Q

It is based on the substrate binding to the active site of the enzyme

A

Kockland’s/Induced Fit Theory

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21
Q

meaning that the enzyme combines with only one substrate and catalyzes only one corresponding reaction.

A

absolute specificity

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22
Q

enzyme combined with all the substrates in a chemical group is called

A

group specificity

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23
Q

enzyme reacting with specific chemical bonds is known as

A

bond specificity

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24
Q

the rate of the reaction is directly
proportional to substrate concentration.

A

first-order reaction

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25
Q

the reaction rate depends only on enzyme concentration

A

zero-order reaction

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26
Q

A method of measurement where the reaction proceeds for a designated time

A

fixed time

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27
Q

A method of measurement where multiple measurements of changes in absorbance are made during the reaction

A

continuous monitoring/kinetic assay

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28
Q

these are nonprotein entities that often bind to particular enzymes and provide a necessary function before a reaction occurs.

A

cofactors

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29
Q

these are organic compound

A

coenzymes

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30
Q

examples of coenzymes

A

NAD and NADP

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31
Q

this may be essential for the reaction or may only enhance the reaction rate in proportion to concentration and it alternates the spatial configuration of the enzyme for proper substrate binding, linking substrate to the enzyme or coenzyme, or undergoing oxidation or reduction.

A

activators

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32
Q

these are inorganic ion attached to a molecule

A

metalloenzymes

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33
Q

metalloenzymes examples are

A

catalase and cytochrome oxidase

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34
Q

it physically binds to the active site of an enzyme but the inhibition is also reversible

A

competitive inhibitor

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35
Q

it does not compete with the substrate but looks for areas other than the active site (allosteric site)

A

non-competitive inhibitor

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36
Q

the inhibitor binds to the enzyme-substrate (ES) complex

A

uncompetitive inhibitor

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37
Q

these are enzymes having the same catalytic reactions but slightly different molecular structures

A

isoenzymes

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38
Q

most physiologic reactions occur in the pH range of

A

pH 7-8

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39
Q

ideal temperature for the preservation of enzymes

A

-20 degree celcius

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40
Q

ideal temperature for the preservation of substrate and coenzymes

A

2-8 degree celcius

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41
Q

ideal temperature for the preservation of LDH

A

22 degree celcius

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42
Q

ALP reference value

A

30-90 U/L

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43
Q

In normal pregnancy increased ALP is detected between

A

16-20 weeks

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44
Q

What blood type have elevated ALP level

A

B and O blood group

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45
Q

In what disease is elevated ALP is seen

A

Paget’s disease

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46
Q

B1x isoform is used to study

A

low bone mineral disease (BMD)

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47
Q

what isoform of ALP is used to study BMD

A

B1x

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48
Q

it is ALP found in the lungs and the most heat stable

A

Regan ALP

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49
Q

Regan ALP is stable at

A

at 65 degrees celsius for 30 minutes

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50
Q

this ALP is inhibited by L-leucine and Phenylalanine

A

Nagao ALP

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51
Q

what isoenzyme of ALP is the most anodal

A

liver and bone ALP

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52
Q

what is used to separate Liver and Bone ALP

A

neuraminidase and wheat germ lectin

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53
Q

heat fractionation /stability test is performed at

A

56 C for 10-15 mins

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54
Q

Decreasing order of ALP heat stability

A

placental, intestinal, liver and bone ALP

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55
Q

Phenylalanine inhibits what ALP isoenzymes

A

placental, intestinal, nagao, and regan ALP

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56
Q

ALP is inhibited by

A

phosphorus

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57
Q

Decreased ALP is seen in

A

zinc deficiency

58
Q

what level of ACP indicates presence of seminal fluid in the sample

A

ACP activity of >50 UI/L

59
Q

ACP is used for the detection of

A

prostatic adenocarcinoma

60
Q

what is used for confirmation of prostatic adenocarcinoma

A

prostate-specific antigen

61
Q

is the specific substrate, and for quantitative endpoint reaction for ACP

A

thymolphthalein monophosphate

62
Q

it is preferred for continuous monitoring method for ACP

A

a-naphthyl PO4

63
Q

what are the two isoenzyme fraction of AST

A

cytoplasmic (predominant) and mitochondrial AST

64
Q

what method is used for AST

A

karmen method

65
Q

it is significant in the evaluation of hepatic disorders

A

ALT

66
Q

what is the coenzyme of aminotransferases

A

pyridoxal phosphate (Vitamin B6)

67
Q

what method is used for ALT

A

coupled enzymatic reaction

68
Q

what is the De Ritis Ratio

A

(ALT:AST) is >1.0

69
Q

what is the S-type and P-type isoenzyme of amylase

A

s-type (ptyalin) and p-type (amylopsin)

70
Q

Salivary amylase is inhibited by

A

wheat germ lectin

71
Q

is an enzyme that hydrolyzes the ester linkages of fats to produce alcohols and fatty acids from triglycerides.

A

lipase

72
Q

it is more pure form of TAG and is used as a substrate for LPS assay

A

Triolein

73
Q

reference method for LPS

A

cherry crandall

74
Q

it is the most commonly used method for LPS; does not use 50% olive oil

A

peroxidase coupling

75
Q

an enzyme that catalyzes the interconversion of lactic and pyruvic acids.

A

lactate dehydrogenase

76
Q

LD isoenzyme for cancer marker

A

LD2, LD3, and LD4

77
Q

predominant LD isoenzyme for cancer marker

A

LD3

78
Q

forward method for LD

A

wacker method

79
Q

reverse method for LD

A

wrobleuski la due

80
Q

increased LDH is seen in what pneumonia

A

pneumocystis jerovecii pneumonia (carinii)

81
Q

catalyzes the transfer of a phosphate group between creatine phosphate and adenosine diphosphate

A

creatine kinase

82
Q

the most anodal ck isoenzyme

A

ck-bb

83
Q

ck mb is not elevated in

A

angina

84
Q

forward method for ck

A

tanzer gilbarg assay

85
Q

reverse method for ck

A

oliver rosalki

86
Q

it interferes with ck assay after release from RBC lysis

A

adenylate kinase (AK)

87
Q

is added to reverse method and inhibit AK intereference

A

adenosine monophosphate

88
Q

it is a marker for alcoholism

A

GGT

89
Q

used as a marker for insecticide poisoning

A

pseudocholinesterase

90
Q

method for PChE

A

ellman technique and potentiometry

91
Q

a possible indicator of neural dysfunction (Alzheimer disease)

A

angiotensin-converting enzyme (ACE)

92
Q

ceruloplasmin is used as a marker for

A

wilson’s disease

93
Q

a marker for hepatobiliary diseases

A

ornithine carbamoyl transferase/carbamyl

94
Q

a newborn screening marker and deficiency of this enzyme leads to drug-induced hemolytic anemia

A

G6PD

95
Q

1 gram of Hb carries

A

1.39 ml of oxygen

96
Q

to minimize ph changes, the lungs maintain what ratio

A

20:1

97
Q

slow or non removal of CO2 increases concentration of

A

Hydrogen ion (H+)

98
Q

increase H+ results to

A

respiratory acidosis

99
Q

decrease H+ results to

A

respiratory alkalosis

100
Q

normal blood ph

A

7.35-7.45

101
Q

normal blood pCO2 level

A

35-45 mmHg

102
Q

normal blood HCO3 level

A

21-28 mEq/L or 22-26 mmol/L

103
Q

caused by bicarbonate deficiency

A

metabolic acidosis

104
Q

it is caused by bicarbonate excess

A

metabolic alkalosis

105
Q

electrolyte imbalance seen in metabolic alkalosis

A

hypokalemia and hypochloremia

106
Q

caused by excessive carbon dioxide accumulation

A

respiratory acidosis

107
Q

caused by excessive carbon dioxide loss

A

respiratory alkalosis

108
Q

anticoagulant for ABG

A

0.05 ml heparin/ml of blood

109
Q

ABG collection method for newborn

A

indwelling umbilical artery catheter

110
Q

what happens to pH, pO2 and pCO2 when standing

A

pH decreases, pO2 decreases, and pCO2 increases

111
Q

these are ions capable of carrying electric charges

A

electrolytes

112
Q

ECF contains

A

1/3 of water

113
Q

ICF contains

A

2/3 of water

114
Q

it is the major EC cation

A

sodium

115
Q

reference value of sodium

A

135-145 mmol/L

116
Q

it promotes sodium retention and potassium excretion

A

aldosterone

117
Q

it is an endogenous antihypertensive agent, and inhibits action of angiotensin II

A

atrial natriuretic factor

118
Q

hypokalemia is seen in

A

cushing syndrome

119
Q

hyperkalemia is seen in

A

addison’s disease

120
Q

method for sodium

A

albanese lein

121
Q

the major IC cation

A

potassium

122
Q

it inhibits Na, K, and ATPase pump

A

Digitalis

123
Q

low insulin causes

A

high serum potassium

124
Q

method for potassium

A

lockhead and purcell

125
Q

polymer membrane of Na

A

TH 227: ETH 157, glass membrane

126
Q

polymer membrane of K

A

Valinomycin gel

127
Q

falsely decreased potassium level is seen in

A

leukocytosis (WBC consume the potassium)

128
Q

falsely increased potassium level is seen in

A

clot formation (platelets releases potassium)

129
Q

it is the major EC anion and chief counter ion of sodium in ECF

A

chloride

130
Q

the only ion to serve as activator

A

chloride

131
Q

method for chloride

A

schales and schales

132
Q

factors affecting plasma calcium levels

A

vit D
parathyroid hormone (PTH)
calcitonin

133
Q

polymer membrane for calcium

A

ETH 1001

134
Q

polymer membrane for chloride

A

lipophilic quaternary ammonium/Ag2S/AgCl

135
Q

causes of hypercalcemia

A

CHIMPS

cancer
hyperthyroidism
latrogenic causes
multiple myeloma
hyperparathyroidism
sarcoidosis

136
Q

causes of hypocalcemia

A

CHARD

calcitonin
hypothyroidism
alkalosis
renal failure
vitamin d deficiency

137
Q

tumor marker for ovarian cancer

A

CA-125

138
Q

tumor marker for breast cancer

A

CA 15-3

139
Q

tumor marker for pancreatic and colorectal cancer

A

CA-19.9

140
Q

tumor marker for lung cancer

A

placental ALP

141
Q

tumor marker for hepatic and testicular cancers

A

AFP

142
Q

tumor marker for urinary bladder cancer

A

nuclear matrix protein

CLINICAL CHEMISTRY (6 decks)

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