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Botany > CC LEC 2 - Enzymes II > Flashcards

CC LEC 2 - Enzymes II Flashcards

1
Q

 128,000 Daltons
 Interconversion of lactic acid and
pyruvic acid

A

LD - Lactate Dehydrogenase

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2
Q

Atypical LD

LD-6: ??

A

alcohol dehydrogenase

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3
Q 
Atypical LD
Migrates cathodal to LD-5
 Present in patients with
arteriosclerotic cardiovascular failure
 Grave prognosis, signifies impending
death
A

alcohol dehydrogenase

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4
Q

Atypical LD

LD complexed with IgA or IgG, migrates between LD-3 and LD-4

A

Macro-LD:

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5
Q

– to measure LD-1(HHHH) because H-units have great affinity

A

*a-Hydroxybutyrate dehydrogenase activity

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6
Q 
Methods for LD
forward reaction
- mixture of phenazine methosulfate
and nitroblue
- tetrazolium reacts with NADH
producing blue purple color
- pH8.3–8.9
A
  1. Wacker method
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7
Q 
Methods for LD
 – reverse
reaction
- NADH is cosubstrate, consumed
during reaction
  • pH7.1–7.6
A

Wroblewski La Due method

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8
Q 
Methods for LD
- 3 times faster, smaller sample, shorter
reaction time
- Susceptible to substrate exhaustion
and loss of linearity
A

Wroblewski La Due method

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9
Q

 Transfer of amino group between aspartic acid and a-ketoacids

A

Aspartate Aminotransferase

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10
Q

ast coenz

A

Pyridoxal phosphate is coenzyme

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11
Q

ast isoenz

predominant form in serum

A

Cytoplasmic Isoenzyme –

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12
Q

ast isoenz

increased during cell necrosis

A

Mitochondrial Isoenzyme

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13
Q 
AST Method
 – coupled enzymatic reaction
- Malate dehydrogenase is indicator enzyme
- Decrease in absorbance at 340nm
- Optimal pH 7.3-7.8
A

Karmen method

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14
Q

AST Method
– ketoacids react with 2,4 – DNPH to form ketoacid hydrazines
- Product is intense brown color measured at 505nm

A

Reitman-Frankel Method

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15
Q
  • Catalyzes transfer of amino groups from alanine to a-ketoglutarate
A

Alanine Aminotransferase

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16
Q

Liver specific enzyme

A

Alanine Aminotransferase

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17
Q

Not elevated in heart disease unless accompanied with liver disease

A

Alanine Aminotransferase

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18
Q

Tends to be higher and lasts longer than AST in acute inflammatory conditions of the liver

A

Alanine Aminotransferase

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19
Q

Requires Mg2+ and Mn2+ as activators

A

Alkaline Phosphatase

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20
Q

class 3 enz

A

ALP

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21
Q

Hydrolysis of various phosphomonoesters; making it nonspecific in alk

A

ALP

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22
Q

ALP isoenz Increased in B and O secretors

A

Intestinal ALP

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23
Q

Abnormal ALP isoenz

A

Regan

Nagao

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24
Q

Abnormal ALP
Variant of Regan
- Detected in metastatic carcinoma of pleural surfaces and in adenocarcinoma of pancreas and bile duct

A

nagao

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25
Q

Abnormal ALP
Highest in ovarian and gynecologic cancers
- Used for monitoring treatment because it disappears upon successful therapy

A

regan

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26
Q

ALP ISOENZ (3) are most heat stable and resist denaturation at 65C for 30 minutes

A

Placental, Regan, and Nagao

27
Q 
inhibits intestinal (75%) and
placental (80%) ALP ISOENZ
A

Phenylalanine

28
Q

Nagao is also inhibited by __

A

L-leucine

29
Q 
inactivates bone(90%0 more
than liver(60%) ALP
A

Urea(2M)

30
Q

Hydrolysis of various phosphomonoesters at acidic pH (5.0)

A

ACP

31
Q

inhibits prostatic ACP

A

Tartrate

32
Q

inhibits non-prostatic ACP

A

Copper

33
Q

__ fastest towards anode; __closer to the cathode

A

pACP fastest towards anode; eACP closer to the cathode

34
Q

Prostatic cancer stage
Small islands of cancer cells in prostate
Normal Population

A

1

35
Q

Prostatic cancer stage
Presence of small nodules in prostate
70-90% live for 5 years

A

2

36
Q

Prostatic cancer stage
Presence of nodes in the prostate and spread around the pelvic area
40-70% live for 5 years

A

3

37
Q

Prostatic cancer stage
Nodules inside and outside prostate, metastasizing in bones and presence of lymph nodes
15-20% live for 5 years

A

4

38
Q

First seen in alcohol intake

A

GGT

39
Q

Transfers gamma glutamyl from gamma glutamyl peptides to Amino Acids, H2O, and other small peptides

A

GGT

40
Q

serves as the gamma glutamyl donor in most biological systems

A

Glutathione

41
Q

is present in large extent in smooth ER and is subjected to hepatic microsomal induction

A

GGT

42
Q

Used as a differentiating source of ALP elevation

A

GGT

43
Q

Mtd of meas for GGT

A

Szasz

44
Q

MW of amylase

A

50 000 - 55 000 daltons

45
Q

Breakdown of starch & glycogen with the products

A

AMS

46
Q

Requires calcium & chloride ions for

activation

A

AMS

47
Q

Tx sources of AMS

A

Acinar cells of pancreas

Salivary glands

48
Q

long, unbranched chain of
glucose molecules, linked by α, 1-4
glycosidic bonds

A

Amylose

49
Q

branched chain
polysaccharide with α, 1-6 linkages
at the branched points

A

Amylopectin

50
Q

similar to amylopectin but more highly branched

A

Glycogen

51
Q

ISOENZ of AMS

  • ## From pancreatic tissue
A

P-type (P1, P2, P3)

52
Q

ISOENZ of AMS

Predominates in urine

A

P-type (P1, P2, P3)

53
Q

ISOENZ of AMS
markedly elevated in acute
pancreatitis & renal failure

A

P3

54
Q

ISOENZ of AMS
From salivary gland tissues, fallopian
tubes, lungs

A

S-type (S1, S2, S3)

55
Q

ISOENZ of AMS

Inhibited by wheat germ lectin

A

S-type (S1, S2, S3)

56
Q

ISOENZ of AMS

Migrates faster than P-type

A

S-type (S1, S2, S3)

57
Q

ISOENZ of AMS
Predominates in serum (2/3 of AMS
activity in serum)

A

S-type (S1, S2, S3)

58
Q

Most commonly observed AMS ISOENZ fractions

A

P2, S1, S2

59
Q

AMS Method
Measures the disappearance in initial dark blue color of starch-iodine complex
- Fast disappearance = high AMS activity

A

Amyloclastic/Iodometric Method

60
Q

AMS Method
Reduction test, reference method
- Starch substrate hydrolyzed by AMS
to its constituent carbohydrate molecule that has reducing properties like sugars
- Amount of reducing sugar = AMS activity

A

Saccharogenic Method

61
Q

AMS Method
Employs a starch substrate with a chromogenic dye that forms an insoluble dye-substrate complex
- With AMS, a smaller soluble fragment of the dye-substrate is formed
- ↑ color intensity of soluble dye- substrate complex = ↑ AMS activity

A

Chromolytic/Chromogen Labelled Substrate Method (Colorimetric)

62
Q

AMS Method

  • Replaced the previous methods in the lab
  • Measures the change in absorbance of NAD+ at 340 nm at pH 6.9
  • Substrate: maltotetrase/maltopentoase
A

Coupled Enzyme Reaction/Continuous Monitoring Method

63
Q

of mg glucose in 30 minutes at 37°C at specific assay conditions

A

Somogyi units:

Botany (324 decks)

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