BIOCHEMISTRY protein Flashcards

1
Q

PH range for pepsinogen

A

1.8 to 3.5

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2
Q

Rennin found in

A

Infants for milk protein caesin digestion

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3
Q

What make active pepsin

A

Hal from parietal cell

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4
Q

What produce pepsinogen

A

Chief cells of stomch

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5
Q

Chief cell aka

A

Zymogenic or peptic cell

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6
Q

Parietal cell aka

A

Oxyntic cell or delomorphous cell

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7
Q

Working of pepsin

A

Break carboxyl end of aromatic aminoacid like tyroosine and phenyl alanine,tryptophan,methionine

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8
Q

Duodenal tissue has

A

Special type of mucosal cell pick up different conc. Of chyme if high in protons, high in carbohydrate,high in protein digesting pdt,fats

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9
Q

Hormones released from duodenum

A

Cholecystokinin,secretin,GIP(gluco insulunotropic peptide)

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10
Q

Digestive enzyme from pancreatic acinus

A

Proteases,amylases,lipases,nucleases

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11
Q

Hormone that induce enzyme secretion from pancreas

A

Cholecystokinin

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12
Q

Optimal ph for pancreatic enzyme activity

A

8

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13
Q

Source of aminoacid

A

Aminoacid metabolism
Trans animation,deamination,glutamase action,pyrimidine metabolism
Action by intestinal bacteria
Aminosugars

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14
Q

Fate of ammonia

A

Synthesis of urea in liver excreated by kidney

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15
Q

What is used for glutamine synthesis

A

Ammonia

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16
Q

Glutamine significance

A
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17
Q

Removal of ammonia from aminoacid by

A

Transanimation

Deamination

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18
Q

Transfer of ammonia from one aminoacid to keti acid and does not reduce free NH3

A

Transamination,deamination

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19
Q

Reduce NH3 from aminoacid

A
20
Q

Exchange of alpha amino group between aminoacid and alpha keti acid by

A

Transamination

21
Q

Interconversion of aminoacid and keti acid in

A

Transamination

22
Q

Aa1+ka2gives

A

Aa2+ka1

23
Q

Enzyme in transamination

A

Transaminase/aminotransferace

24
Q

Coenzyme needed

A

Pyridoxyl phosphate

Vitamin b6

25
Q

Transamination os irreversible or reversible

A

Reeversible

26
Q

Free NH3 not generated in

A

Transamination

27
Q

Major transaminase in body are

A

AST&ALT

28
Q

Major amount of transaminase

A

Liver ,kidney,muscle&brain

29
Q

Acceptor of keto acid result in formation of glutamate

A

Alphoketoglutarate

30
Q

Collecting point of all alpha aminogroup

A

Glutamate

31
Q

What is deamination

A

Release of ammonia

32
Q

Why Glutamate undergo oxidative deaminationtion to liberate free NH3

A

For urea synthesis

33
Q

Thae amino acids that do not participate in transamination

A

Lysine,threonine,proline,

34
Q

Why transamination is reversible

A
35
Q

Significance of transamination

A

Removal of ammo ia by aminoacid,synthesis of nonessential aminoacid like alanine from pyruvate,interconversion of aminoacid to equal concentration
No energy generayed

36
Q

Clinical significance of transamination

A
37
Q

Patient with liver disease antibiotics given. why?

A

To kill intestinal bacteria that they are important source ammonia in body

38
Q

Deficiency of oxaloacetate increase catabolism of which potential energy source

A

Glucogenic aminoacid

39
Q

Pyridoxyl phosphate derived from

A

Vit b12

40
Q

Pyridoxyl phosphate link with enzyme like schiff base linkage

A

Schift base linkage

41
Q

Schiff base means

A

Ketone replaced by Imine or m ethine group

42
Q

Enzyme used for al anne transamination

A

Alanine amino transaminase/transferase

43
Q

Transamination of alanine and alpha keto glutarate gives

A

Pyruvate and glutamate

44
Q

Fate of pyruvate

A

Lactic acid(cori cycle),acetyl co A(krebs cycle,ETC)

45
Q

glucose 6 phosphate convert to glucose in liver due to its unique enzyme

A

Glucose 6 phophphatase