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S.N Biochemistry 3 > LABS- 2nd semester > Flashcards

LABS- 2nd semester Flashcards

1
Q

what is the structure of lactate DH?

A

tetramer

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2
Q

which LDH isoenzyme found in the heart?

A

LDH1

LDH2

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3
Q

what is the location of LDH5?

A

liver

smooth muscle cell

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4
Q

write down the reaction catalyzed by LDH-

A

pyruvate + NADH + H -> lactate + NAD

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5
Q

what is the optimal lactate conc for LDH1 and LDH5?

A 
LDH1= 10mM
LDH5= 250 mM
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6
Q

what happens to LDH1 in the presence of 250mM lactate?

A

it is inhibited by 50%

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7
Q

what is the different substrate specificity btw. LDH1 and LDH5?

A 
LDH1= 2-oxobutyrate
LDH5= pyruvate
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8
Q

which enzyme is fastest in the electric field separation method?

A

LDH1

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9
Q

what is the prosthetic group of transaminase?

what is it derived from?

A

PLP

B6

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10
Q

describe the reaction catalyzed by Asp-AT

A

Asp+aKG -> OAA+Glu

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11
Q

where does Asp-AT localized?

where is it conc very high?

A

all organs

high conc in liver and heart

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12
Q

describe the reaction catalyzed by Ala-AT

A

Ala+aKG -> pyruvate+Glu

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13
Q

where does Ala-AT localized?

where is it activity very high?

A

liver- high activity
kidney
heart
skeletal m

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14
Q

what is the reaction catalyzed by MDH (malate DH)?

A

OAA + NADPH +H -> malate + NAD

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15
Q

in both experiments of ALAT and ASAT, what do we check?

A

we check the amount of NADH that was transfered to NAD (ill person is faster)

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16
Q

in what disease does the levels of ASAT elevates more than ALAT?

A

myocardial infraction

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17
Q

in what disease does the levels of ALAT elevates more than ASAT?

A

hepatocellular tissue destruction

remember, ALAT is with L, like the Liver

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18
Q

write down the reaction catalyzed by creatine-kinase

A

ATP + creatine -> ADP + creatine-P + H

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19
Q

where can we detect high amounts of creatine-kinase?

A

muscle
heart
brain

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20
Q

what is the structure of creatine-kinase?

A

dimer (two subunits)

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21
Q

describe the 2 subunits of creatine-kinase

what isoenzymes do they produce?\

A

CK-M
CK-B
produce 3 isoenzymes (CK-MM, CK-BB, CK-MB)

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22
Q

connect each creatine-kinase isoenzyme to its organ

A

CK-MM: muscle
CK-BB: brain
CK-MB: heart

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23
Q

which enzymes activity play a crucial role in the verification of myocardial infraction?

A

CK
LDH
LDH1
ASAT

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24
Q

what is the normal range of fasting glucose levels?

A

3.5-5.5 mM

25
Q

in a healthy person, when can we see the highest blood glucos levels? (after a glucose load)

A

after 1 hour

26
Q

what value of fasting plasma glucose indicates diabetes?

A

more than 7mM

27
Q

what drug will inhibit Na/K ATPase?

A

Ouabain

28
Q

how can we determine the Na/K ATPase activity?

A

by assaying the amount of liberated inorganic phosphate using the Fiske-Subbarow colour reaction

29
Q

what is the perpose of biotransformation?

A

conversion of foreign (xenobiotics) compounds to water soluble substance
excretion out of the body

30
Q

where does tthe CYP P450 localyzed?

A

in the ER membrane

31
Q

what happens in the CYP P450 system?

A

electrons are transfered from NADPH to FAD prosthetic group of CYP P450 reductase enzyme, and from FMNH2 electrons flow to CYP P450 hemoproetin to reduce ferric ion

32
Q

what does microsome contains?

A

plasma membrane
ER
membrane fragments (rich in CYP enzyme system)

33
Q

what is the most frequent reaction catalyzed by CYP P450?

A

hydroxylation

34
Q

give example of a compound that will induce many kinds of CYP isoenzymes?

A

polycyclic aromatic hydrocarbons

35
Q

what is aminophenazone?

what will happend to it?

A

antipyretic nonsteroidal anti-inflammatory drug

this compound will demethylated and will produce formaldehyde and free -NH2 remains on the drug

36
Q

what is the end product of blood coagulation?

A

fibrin gel

37
Q

what is the composition of fibrinogen?

how are they bound?

A

2Aa
2Bb
2gamma
they are bound with disulfide bbonds

38
Q

what type of enzyme is the thrombin?

A

serine protease

39
Q

what does the thrombin cleave?

what is the product?

A

peptide bond in the Aa chain and the Bb chain

products are- fibrinopeptide A+B and fibrin I+II monomer

40
Q

what activates factor XIII?

what does it do?

A

thrombin
glutamyl-lysyl amide cross links (isopeptide bond)
btw a and gamma chains of the monomers

41
Q

what is the aim of the succinate DH lab?

A

determine whether malonate is a cometative inhibitor for succinate DH

42
Q

describe competative inhibitor

what happens to the Km?

A

binds reversibly to the free enzyme
enzyme-inhibiroe has no catalytic activity
Km increases

43
Q

write down the reaction catalyzed by succinate DH

A

succinate + FAD -> fumarate + FADH2

44
Q

why malonate can be succinate DH substrate analogue?

A

similar structure to succinate

45
Q

what is special about succinate DH?

A

it is the only inner mitochondrial membrane-bound enzyme of the citric acid cycle

46
Q

why do we use INT in the succinate DH experiment?

A

to make the reaction irreversible
it is an artificial acceptor
end product is red colored

47
Q

describe what is the P/O ratio

A

number of ATP synthesized per oxigen consumed

48
Q

what is special about the M-type pyruvate kinase?

A

(muscle)
shows no allosteric behavior
only under high ATP conc. it may be inhibited

49
Q

how did we measure the activity of pyruvate kinase in the lab?

A

rate of conversion of PEP to pyrubate is coupled to lactate DH.
we measure the amount of NAD+ produced (pyruvate->lactate)

50
Q

which form absorbs the light in 340 nm?

NADH/NAD+

A

NADH

51
Q

how does pancreatic lipase activates?

A

colipase
in the duodenum (pH dependant)
alsombile acids enhance the activity of thr lipase enzymr (in the presebcr of colipase)

52
Q

describe the experiment of pancreatic lipase, what did we check?

A

lipase+colipase+milk

we compared results in the presence of water/presence of bile acids

53
Q

how did we evaluate the pancreatic lipase action?

A

value of NaOH required to neutralize the milk is directly related to the presence og TAG and hence the enzyme activity (we will see that is is hugher in the presence of bile acids)

54
Q

what is the cause for primary carnitine deficiency?

A

mutation un the gene coding OCTN2 that transports carnitine into cells

55
Q

in the laboratory practice the determination of the serum cholesterol level is assayed by the measurments of

A

formation of quinoneimin

(H2O2+phenol_amino-4-antipyrin->quinoneimine+2H2O catalyzed by peroxidase

56
Q

what are the enzymes that weree used in our experiment of determined serum TAG?

A

lipoproein lipase
glycerol kinase
glycerol-3-P-oxidase
peroxidase

57
Q

what are the enzymes that weree used in our experiment of determined cholesterol?

A

cholesterol esterase
cholesterol oxidase
peroxidase

58
Q

what is the only inner mitochondrial membrane bound enzyme of the TCA?
what is it competitive inhibitor?

A

succinate DH

malonate

59
Q

the reaction of succinate DH is measured by the following compound

A

reduced idonitrotetrazolium formazan which is red

S.N Biochemistry 3 (14 decks)

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