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
Q

In chronological order, what ALP isoenzyme is the fastest?

A

Liver > Bone > Placental > Intestinal Isoenzyme

26
Q

What are the methods for the separation of Isoenzymes?

A
  1. Inhibition
  2. Heat fractionation
  3. Electrophoresis
  4. Use of enzymes or lectins
27
Q

ALP elevation happens if there is?

A
  • Obstructive hepatic disorders
  • Paget’s disease
  • B1x
  • DM, renal failure and cirrhosis
  • ALP isoenzymes in cancer patients
28
Q

In extensive obstruction, there will be ________increase in the ULN of ALP.

A

3 FOLDS

29
Q

This refers to the bone ALP isoform in the serum of dialysis patients.

A

B1x

30
Q

What ALP isoenzyme will increase in DM, renal failure and Cirrhosis?

A

Increased Intestinal ALP

31
Q

Physiological elevation are seen during?

A
  1. Pregnancy
  2. Infant and Children
32
Q

Physiological elevation are seen during?

A
  1. Pregnancy
  2. Infant and Children
33
Q

In infants and Children, how many times is the elevation?

A

10x

34
Q

What ALP isoenzyme is present in Infants and Children?

A

Liver and Bone isoenzymes

35
Q

This isoenzyme is present to patients with a particular type of lung CA.

A

Regan Isoenzyme

36
Q

This isoenzyme is present to patients that have adenocarcinoma

A

Nagao Isoenzyme

37
Q

This is present to patients that have hepatoma.

A

Kasahara isoenzyme