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ALP Flashcards

1
Q

What is the known function of ALP?

A

Lipid transfer in the intestine and bone formation

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2
Q

This hydrolyzes naturally occurring substrate.

A

ALP

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3
Q

What is the optimum pH of ALP?

A

10.3

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4
Q

What is the systematic name of ALP?

A

E.C. 3.1.3.1

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5
Q

What are the major isoenzymes of ALP?

A
  1. Placental Isoenzyme
  2. Intestinal Isoenzyme
  3. Liver Isoenzyme
  4. Bone Isoenzyme
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6
Q

What method is used for ALP measurement?

A

Bowers and McComb

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7
Q

This method uses p-NPP substrate. Thus, chelators falsely lower activity. First, enzyme activity increases slightly on storage and is relatively stable at 4’C up to a week.

A

Bowers and McComb

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8
Q

In storage, at what rate does enzyme activity increase per day?

A

2%

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9
Q

Under Bowers and McComb, enzyme activity will remain stable at what temperature?

A

4’C up to a week.

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10
Q

If the sample is frozen. What should we do?

A
  1. Thaw
  2. Store the sample at RT for 18 - 24hrs before testing.
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11
Q

If the sample is frozen. What should we do?

A
  1. Thaw
  2. Store the sample at RT for 18 - 24hrs before testing.
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12
Q

ALP reaction only takes place in the presence of cofactors (disulfide ions). What are these?

A
  1. Cobalt
  2. Magnesium
  3. Manganese
  4. Zinc
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13
Q

This cofactor serves as a constituent metal ions and must combine with ALP reaction to take place because without this factor ALP reaction would be incomplete.

A

Zinc

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14
Q

What are the Inhibitors of ALP?

A
  1. Phosphates
  2. Borate
  3. Oxalate
  4. Cyanide ions
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15
Q

If the anticoagulant contains these inhibitors, it should never be used in measuring ALP. What are these?

A

Borate and Oxalate

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16
Q

What isoenzymes do this inhibit?
A. Phenylalanine
B. Levamisole

A

A. Intestinal and Placental
B. Liver and Bone

17
Q

This separation of enzymes is differentiated based on heat stability.

A

Heat fractionation.

18
Q

In heat fractionation, at what degrees is the enzyme exposed to?

A

56’C for 10 minutes

19
Q

What isoenzyme is separated in Heat Fractionation?

A

All except Intestinal Isoenzyme

20
Q

In electrophoresis, it is exposed to what enzyme?

A

Neuraminidase

21
Q

In electrophoresis, what are we going to do with the neuraminidase?

A

For 15 minutes, pretreat the neuraminidase + serum @ 37’C

22
Q

What are the substrates used in Electrophoresis?

A
  • Agarose gel
  • Polyacrylamide gel
  • Cellulose acetate
23
Q

This improves separation of bone and liver form. Differences in their CHO side chains.

A

Use of enzymes or lectins

24
Q

What overlaps with bone isoenzyme?

A

Placental Isoenzyme

25
In chronological order, what ALP isoenzyme is the fastest?
Liver > Bone > Placental > Intestinal Isoenzyme
26
What are the methods for the separation of Isoenzymes?
1. Inhibition 2. Heat fractionation 3. Electrophoresis 4. Use of enzymes or lectins
27
ALP elevation happens if there is?
- Obstructive hepatic disorders - Paget's disease - B1x - DM, renal failure and cirrhosis - ALP isoenzymes in cancer patients
28
In extensive obstruction, there will be ________increase in the ULN of ALP.
3 FOLDS
29
This refers to the bone ALP isoform in the serum of dialysis patients.
B1x
30
What ALP isoenzyme will increase in DM, renal failure and Cirrhosis?
Increased Intestinal ALP
31
Physiological elevation are seen during?
1. Pregnancy 2. Infant and Children
32
Physiological elevation are seen during?
1. Pregnancy 2. Infant and Children
33
In infants and Children, how many times is the elevation?
10x
34
What ALP isoenzyme is present in Infants and Children?
Liver and Bone isoenzymes
35
This isoenzyme is present to patients with a particular type of lung CA.
Regan Isoenzyme
36
This isoenzyme is present to patients that have adenocarcinoma
Nagao Isoenzyme
37
This is present to patients that have hepatoma.
Kasahara isoenzyme

CLINICAL CHEMISTRY 2 (23 decks)

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