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CLIN CHEM > ENZYMES INTRO/CK/LDH > Flashcards

ENZYMES INTRO/CK/LDH Flashcards

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1
Q

Enzymes

— _______; is a biological substance that catalyzed a reaction [make the chemical reaction faster]
􏰀 When the enzymes are absent, the reaction would continue but _______.

— Location of enzymes: within the cells [______, ______,intestines and stomach]

􏰀 Cellular injury/degradation → the enzymes would be ?

  • Detection of _____ when certain enzymes are high.
A

biocatalyst

slower

saliva
pancreas

released into circulation

disorder

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2
Q

Essential to Physiologic Functioning:
✔ Hydration of _____—> ____ maintenance of the blood. as hydrogen can combine with it as acidic/ basic substances.

✔ _______ conduction
✔ ________ contraction
✔ ________ degradation􏰀 found in _____ tract [______, _____]
✔ _______ use

A

CO2
pH maintenance

Nerve conduction
Muscle contraction
Nutrient degradation [GI: amylase, lipase]
Energy use

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3
Q

For a fast chemical reaction to occur, there must be the presence of ________[enzymes] + _________.

● _________ site [the substrate]— water-free cavity, where the substance on which the enzyme acts
- ideal environment, such as a slightly [basic/acidic] or [polar/non- polar] environment, for the reaction to occur.

o _________ complex— fast chemical reaction
● _________ site— area other than the active site: water- free

A

reactants
substrates

Active
basic
non-polar

ES
Allosteric

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4
Q

A chemical reaction may occur spontaneously if the [2] is higher for the reactant than the products.

􏰀 _________— reactants have enough energy to break their bond and collide to form new bond [bond between the enzyme & substrate]

A

free energy [reactants]
available kinetic energy

Activation Energy

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5
Q

􏰀 _________ Specificity– [strictest] enzyme + only 1 substrate and catalyzed a single reaction

􏰀 _________ Specificity– + all substrates containing a particular chemical group

􏰀 _________ Specificity– other enzymes are specific to chemical bonds [hydrogen bonds]

􏰀 _________ Specificity + predominantly combine with only 1 optical isomer [mirror image] of a certain compound.

A

Absolute

Group

Bond

Stereoisomeric

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6
Q

_________: gen. temperature for preservation

_________: long term preservation

_________: for cold-labile enzymes
Examples [2]

_________ temperature– reversible inactivation enzyme

_________= NOT RECO → inactivates the enzymes

A

-20C

2-8C

RT
LD4,LD5

Cold temperature

Repeated Thawing

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7
Q

Enzymes that increase in terms of hemolysis:

A

KLAMP
potassium
LDH
AST
ACP
Aldolase
Magnesium
Phosphate/Phosphorus

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8
Q

A lactescence and milky specimen means that there is a [INC/DEC] in concentration, and there is the presence of______.

A

DEC

chylomicrons

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9
Q

Once the counterpart reactant is saturated, and an additional reactants are applied, what will happen to the reaction?

A

it will not result to faster reaction

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10
Q

In substrate and enzyme concentration, it follows the hypothesis of _______ “even in low substrate conc→ the substrate can ______with free enzyme”

A

Michaelis & Menten

readily bind

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11
Q

Enzymatic Reaction can be:
✔ _________– the rxn rate is directly proportional to substrate concentration.

✔ _________– rxn rate depends only on enzyme concentration.

A

First Order kinetic

Zero Order Kinetic

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12
Q

In First Order Kinetic, there is the addition of more _______ to easily find its counterpart.

In Zaro Order Kinetic, there is the addition of more _______ to easily find its counterpart.

A

substrate

enzyme

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13
Q

_________Enzymes are protein that carry a net molecular charge

— # physiologic enzymatic reactions occur in the pH range of _________ but some enzymes are active in wider pH ranges than others.
[2 Examples]

A

pH

7.0-8.0

ACP- acid
ALP- basic

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14
Q

TEMPERATURE
[INC] = [INC/DEC] chemical rate rxn

Temperature coefficient
– In every increase of [#] degree = [#]x increase rate rxn; until, of course, the
________ is denatured.

________– optimum temp.
________— [INC] denaturation rate increases as the temp
increases and is usually [significant/nonsignificant]

________— enzymes inactivation _______temperature— enzymes inactive
- ___________→ prevent activity loss until analysis.

A

10 degree
2x
protein

37C
40-50%

60-65%
Low
Frozen/Refrigerated

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15
Q

___________ non-protein entities that must bind with enzyme for a rxn to occur

  1. ___________—made up of inorganic cofactors
    — function by alternating the enzyme ___________ [enzyme ___________ change that corresponds to the substrate] for proper substrate binding

—Linking substrate to the enzyme/coenzyme, or undergoing ___________.

✔ Metallic: [5]
✔ Non-metallic: [2]

A

COFACTORS

Activatiors
spatial configuration
shape

oxidation-reduction

Ca, Fe, Mg, Mn, Zn, K
Br, Cl

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16
Q

___________— made up of organic cofactors
— as 2nd substrates for enzymatic rxn.
▪ ___________ between the enzyme and substrate [↑ ___________ of the rxn]

___________– when bound tightly to the enzyme, coenzymes
o E.g. [3]

A

Coenzymes

Bridge
velocity

Prosthetic groups
Vit, NAD, NADP

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17
Q

Interfere with the reaction= Enzymatic reactions may not progress normally

A

Inhibitors

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18
Q

physically bind to the active site of an enzyme and compete with the substrate for the active site.
[same shape with the active site= NO ES complex formed]

A

Competitive Inhibition

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19
Q

Is competitive inhibition reversible or not? If yes, how?

A

Reversible

By increasing the substrate concentrate, so the possibility of its binding capacity is higher than the inhibitor.

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20
Q

binds an enzyme at a place other than the active site [allosteric site]= NO ES complex produced= NO RXN CATALYZED

A

Non-competitive Inhibition

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21
Q

Is Noncompetitive inhibition reversible, irreversible or both? explain.

A

Both

Reversible, by other substances that can bind other than the inhibitors.

Irreversible, when the inhibitors destroys the active site.

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22
Q

True or False

In NonCompetitive Inhibition, Increasing the substrate concentration would not reverse the reaction as it binds the enzyme independently from the substrate [binds to allosteric site]

A

True

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23
Q

inhibitor binds to the ES complex.

A

Uncompetitive Inhibition

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24
Q

2 METHODS IN MEASURING THE ENZYMATIC RXN
— Measure based on their _______ and not the absolute ______.
[2]

A

activity

value

Fixed-time/End point
Continuous Monitoring/Kinetic Assay

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25
Q
  1. _____________ – single measurement of sample

—– reactants are combined → rxn proceeds for a designated
_______ → rxn stopped [most enzyme inactivation is by the help of _______]

A measurement is made of the ________ that has occurred
[larger reaction= more enzymes are present]

A

Fixed time/End point

time
weak acid

amount of reaction

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26
Q

_________________ Assay– multiple measurement of enzyme activity at specific time intervals

A

Continuous monitoring/Kinetic assay

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27
Q

Continuous Monitoring/Kinetic Assay is preferred because?

It is also the most common deviation where enzyme is so ________ → all ________ is used early in the reaction time.

A

any deviation from linearity is readily observable

elevated
substrate

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28
Q

results in structural cavities.

A

Tertiary structure

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29
Q

made up of polypeptide chain twisting

A

Secondary structure

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30
Q

enzyme contains more than one polypeptide unit: spatial relationships between the subunits

A

Quarternary structure

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31
Q

Catalyze an oxidation–reduction
reaction between two substrates

Catalyze the transfer of a group other than hydrogen from one substrate to another

Catalyze hydrolysis of various bonds
o Breaks substances with the use of _______.

A

Oxido-reductase

Transferase

Hydrolase

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32
Q

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

A

Lyase

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33
Q

Catalyze the interconversion of geometric,
optical, or positional isomers

A

Isomerase

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34
Q

Catalyze the joining of two substrate molecules,
coupled with breaking of the ____________ bond in ATP or a similar compound

A

Ligases
pyrophosphate

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35
Q

digit of subclass and sub-subclass

A

2nd + 3rd

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36
Q

digit of class

A

1st

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37
Q

digit of the serial number specific to each enzyme in a sub- subclass

A

4th

38
Q

Dimer w/ 2 subunits

A

CK Isoenzymes

39
Q

Dimer w/ 2 subunits
Enzymes with same catalytic function but DIFF physical PROPERTIES.

A

CK Isoenzymes

40
Q

Percentage from the total CK:

CK1/BB-
CK2/MB-
CK3/MM-

A

1%

<6%

94-100%`

41
Q

CK that is of :
Brain type: Brain tissue

A

CK-BB

42
Q

CK that is hybrid type [muscle + brain]: more on from the _______.

A

CK-MB/2

heart

43
Q

CK that is muscle type: mostly ______ muscle [Examples]

A

CK-MM/3

skeletal

LD1-5

44
Q

— Associated w/ ATP generation in contractile system and is related with muscular system

A

Creatine Kinase/Phosphokinase

45
Q

CK function in the muscle cells, it stores Creatine phosphate that is important in ______ production.

A

ATP

46
Q

Creatine Kinase/Phoshphokinase is differentiated by 3 methods:

A

Electrophoresis
Solubility
Inactivation resistance

47
Q

CK’s arrangement in electrophoresis.
[from cathode to anode]

A

Cathode- CK3- CK2- CK1- Anode

48
Q

— Seldomly found in the plasma
Short half life: 1-5 hrs

A

CK-BB

49
Q

_____________
Have a high molecular size → cannot pass through
the x Blood Brain Barrier → Confined to the ______ or ______.

A

CK-BB

brain
cranium

50
Q

May be seen in the circulation of neonates as this is not developed fully.

A

CK-BB

51
Q

— MOST IMPORTANT part of CK

A

CK-MB

52
Q

A tissue that compromises 20% of CK-MB and very little to other tissues

A

Cardiac tissue

53
Q

is the only tissue from which CK-MB enters the serum, meaning it is quite specific to the ________ muscle

A

Myocardium
cardiac

54
Q

CK-MB as indicator of AMI
􏰀 Rise= _______
􏰀 Peak= _________
􏰀 Normalize= ________

A

4-8 hrs
12hrs-1day
2-3days

55
Q

􏰀 Other cardiac markers aside from CK-MB: [3]

A

LDH
AST
Troponin

56
Q

— SERUM MAJOR FRACTION 􏰀 @ Skeletal/Cardiac muscle

A

CK-MM

57
Q

CK- MM
[INC]: [3]

A

Hypothyroidism
IM Injection
Muscle activity

58
Q

o Hypothyroidism: [INC] ___________ + [DEC] ________ due to slow _________
o Muscle activity: __________
o IM: ___________

A

membrane permeability
CK clearance
slow metabolism

vigorous exercise
muscle damage

59
Q

MACRO-CK
– midway between MM AND MB
– related to age and sex: associated to ____________.

2 FORMATION THEORIES:
- CK ____ that is found in IgG
- CK ____ that is bound to
lipoprotein

􏰀 NO clinical significance

A

MACRO-CK

age, sex

> 50 yrs old female

BB
MM

60
Q

________________
— Found before MM.
— Bound to the exterior surface of mitochondrial membrane of [3]

Clinical significance: [3]

A

Mitochondrial CK [CK-Mi]

mitochondrial
muscle
brain,
liver

severe illness
malignant tumors
cardiac abnormalities

61
Q

Hypothyroidism, malignant hyperpyrexia, Reye’s syndrome, Vibrio Vulnificus — are clinically significant to what CK?

A

CK-MM

62
Q

METHODS USED FOR THE MEASUREMENT OF ISOENZYMES OF CK
[4] [+2 subtypes]

A
  1. Electrophoresis
  2. Ion Exchange Chromatography
  3. Ab used for CK MB/AMI Diagnosis
  4. Immunoassay
    – Tanzer-Gilbarg Assay
    –Oliver- Rosalki Assay
63
Q

REFERENCE method of CK

A

Electrophoresis

64
Q

More SENSITIVE, PRICY > electrophoresis

Problem with the _______:
CK-____ merge with CK-____
CK-____ eluted with CK-____

A

Ion exchange chromatography

Bad column
BB
MB

MM
MB

65
Q

__________ inhibits ALL the activity of M subunit.

o _________: 2 Subunits M
- entire activity would be
inhibited
o _________: 1 M subunit
- half of the activity would be inhibited

▪ B is left
▪ CK B Activity X [#] = reflect CK___ activity

o _________: NO M subunits
- not affected; isolated to
the _______

A

Anti-M antibody

CK3

CK2

2x

CK1
brain

66
Q

􏰀 Detects MB reliably with minimal reactivity
􏰀 Detects enzyme protein rather than activity

A

Immunoassay

67
Q

In immunoassay for CK, with RBC hemolysis, it will release __________= resulting to falsely [increased/decreased] values of CK

A

Adenylate kinase/AK

increased

68
Q

CK IMMUNOASSAY
Storage:

_____C: CK may last for up to 7 days
_____: CK may last for 1 month

Reference values: Total CK Male: ______U/L
- much muscular >
Female: _____ U/L

A

-20C

4

15-160
15-130

69
Q

TANZER-GILBARG ASSAY
[_____pH @340 nm]
[Forward/Direct reaction or Reverse/Indirect reaction]

OLIVER-ROSALKI ASSAY
[_____pH @_____ nm)
[Forward/Direct reaction or Reverse/Indirect reaction]

A

9.0pH
Forward/Direct

6.8 pH
340
Reverse/Indirect

70
Q

Reactions in:
Tanzer Gilbarg

A

Creatine + ATP –[CK]– Creatine phosphate + ADP

ADP + Phoshoenol pyruvate —ATP + Pyruvate

Pyruvate + NADH + H –[LD]– Lactate + NAD

71
Q

Reactions in:
Oliver Rosalki Assay

A

Creatine phosphate + ADP –[CK] – Creatine + ATP

ATP + glucose – ADP + G6P

G6P + NADPH– [GDPD]– 6phosphogluconate + NADP

72
Q

Catalyzes the interconversion of lactic acid and pyruvic acid
o Lactate + ______ —> Pyruvate + ______.
Coenzyme: ________.

A

Lactate dehydrogenase

NAD
NADH

NAD

73
Q

Tetrametric molecules containing 4 subunits of 2 possible forms [H-heart, M-Muscle]

A

LD Isoenzymes

74
Q

LD HHHH & LD HHHM are indicators for these 2 conditions

A

heart, RBC

AMI
Intravascular hemolysis

75
Q

LD HHMM is an indicator for this condition

A

pulmonary disorders
[pulmonary carcinoma]

76
Q

LD HMMM is an indicator for this condition

A

intrahepatic disorder

77
Q

LD MMMM is an indicator for this condition

A

muscular dystrophy

78
Q

Abnormal type of LD Isoenzymes
✔ _____ Band to the electrophoresis
✔[2 conditions] → could lead to ______ damage.

A

6th

impending death
arteriosclerotic cardiovascular failure

liver

79
Q

LD isoenzyme designated for liver

A

LD HMMM/4

80
Q

LD isoenzyme designated for lungs, lymphocyte, spleen, pancreas

A

LD HHMM/3

81
Q

LD isoenzyme designated for the skeletal muscle

A

LD MMMM/5

82
Q

LD isoenzyme designated for heart and RBC

A

LD HHHH/1
LD HHHM/2

83
Q

LD is NON-SPECIFIC, thus it should be differentiated through their concentration.
[Concentration order from highest to lowest]

  • LD 1& 2 have same tissue sources but LD___ has more.

_____________
–Concentration of LD1 becomes higher than LD2.
–Indicates [2]

A

LD2–LD3–LD1–LD4–LD5

1

Flipped pattern

AMI
Hemolyzed sample

84
Q

MEASUREMENT OF LD ISOENZYMES

A

Electrophoresis
Immunoinhibition/Chemical Inhibition
Substrate affinity

85
Q

DIAGNOSTIC SIGNIFICANCE
LDH is increased in these 6 disorders:

[Highest] in: [2]
- LDH is a ______ marker

A

Renal disorder
Hepatic disorder
Cardiac disorder
Skeletal disorder
Hematologic disorder
Neoplastic disorder

pernicious
hemolytic disorder AMI

Cardiac

86
Q

LDH in AMI
- Rise: _____ hrs
- Peak: _____ hrs
- Normalize: _____days

A

12-24hrs
48-72hrs
10 days

87
Q

LDH Isoenzymes METHODS [2]

A
  1. Wacker
  2. Wrobleuski and La Due
88
Q

Reference value of LDH

A

100- 225 U/L

89
Q
  1. Wacker Method [_____ pH @ 340 nm]
  2. Wrobleuski and La Due [______pH @_____nm]
A

8.3-8.9 pH

7.1-7.4 pH
340nm

90
Q

__________________.
✔ 3X faster > to wacker method, [small/large] sample is needed
✔ Susceptible due to [2]

✔ HEMOLYSIS should be prevented because?

o LDH is a ______ labile
􏰀 use ____ in storage
▪ LD___ is the MOST LABILE.

A

Wrobleuski and La Due

small

substrate exhaustion
loss of linearity

RBC contains 100-150x the LDH concentration.

cold
RT
5

91
Q
A

CLIN CHEM (12 decks)

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