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Clinical Chemistry (CC 1) > (F) L1: Enzymes (Part 2) > Flashcards

(F) L1: Enzymes (Part 2) Flashcards

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1
Q

Major Clinical Enzymes: Phosphatases

  • Aka “Alkaline Orthophosphoric Monoester Phosphohydrolase”
  • Is non-specific
  • Is active in a pH of 10 to 15
  • It liberates inorganic phosphate with a byproduct of alcohol
A

Alkaline Phosphatase (ALP)

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2
Q

Alkaline Phosphatase

What are the 5 major tissue sources of ALP?

A
  1. Liver
  2. Bone
  3. Placenta
  4. Intestine
  5. Kidney
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3
Q

Alkaline Phosphatase

Order the tissue sources from most abundant to least abundant:

  • Placenta
  • Intestine
  • Liver
  • Bone
  • Kidney
A
  1. Liver (major source)
  2. Bone (major source)
  3. Placenta
  4. Intestine
  5. Kidney (minor source)
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4
Q

Alkaline Phosphatase

An increase in bone isoenzyme is seen in what 2 age groups?

A
  1. Growing children
  2. Geriatric patients (>50 years old)

For children, since they are continuously undergoing bone resorption, bone tissues are continuously destroyed which liberates the enzymes

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5
Q

Alkaline Phosphatase

An increase in ALP can also be seen in pregnant women how many weeks along in their pregnancy?

A

16-20 weeks

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6
Q

Alkaline Phosphatase

ALP is affected by an individual’s blood type (choose among ABO):

  1. Increase in intestinal isoenzyme after a fatty meal
  2. Decrease in intestinal isoenzyme after a fatty meal
  3. Decrease in placental isoenzyme for pregnant women
A
  1. B and O
  2. A and AB
  3. A and AB
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7
Q

Alkaline Phosphatase

What is the reference value?

A

30-90 U/L

Subjected to changes depending on multiple factors such as age, sex, race, and others

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8
Q

Alkaline Phosphatase

What are the 4 major clinical isoenzymes?

A
  1. Placental ALP
  2. Intestinal ALP
  3. Liver ALP
  4. Bone ALP
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9
Q

Alkaline Phosphatase (Specimen Considerations)

Match the elements with their functions:
1. One of the major components of ALP
2. An activator required in the analysis
3. An inhibitor

A. Phosphorus
B. Zinc
C. Magnesium

A
  1. B
  2. C
  3. A
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10
Q

Alkaline Phosphatase (Specimen Considerations)

In order to bind and inhibit phosphorus (since it is already a normal serum component), what buffer must be used?

A

2-amino-2-methyl-1-propanol (AMP)

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11
Q

Alkaline Phosphatase (Specimen Considerations)

Does ALP increase or decrease after these activities/events?
- Hemolysis
- After ingestion of fatty meals (or food in general)
- Sample stored at 4ºC

Note: Fasting is not required for ALP testing

A

Increase

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12
Q

Alkaline Phosphatase (Methods of Analysis)

This separates the different isoenzymes of ALP since each type exhibits different migrating patterns

A

Electrophoresis

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13
Q

Alkaline Phosphatase (Electrophoresis)

What is/are the most anodal and least anodal isoenzymes?

Choose between: Liver, Bone, and Intestinal

A
  • Most anodal = Liver and Bone
  • Least anodal = Intestinal
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14
Q

Alkaline Phosphatase (Electrophoresis)

What is Neuraminidase and Wheat Germ Lectin’s role in electrophoresis?

A

Separating agents for the separation of bone and liver ALP

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15
Q

Alkaline Phosphatase (Electrophoresis)

High resolution electrophoresis using polyacrylamide gel with isoelectric focusing is used for what purpose?

A

To separate multiple overlapping ALP bands

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16
Q

Alkaline Phosphatase (Methods of Analysis)

This exposes enzymes at 56ºC for 10-15 minutes wherein the most stable enzyme will persevere

A

Heat Fractionation/Stability Test

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17
Q

Alkaline Phosphatase (Heat Fractionation/Stability Test)

Rank the ALPs from most heat stable to most heat labile?

Choices: Bone, Placenta, Intestinal, and Liver

A

Placental, Intestinal, Liver, Bone

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18
Q

Alkaline Phosphatase (Methods of Analysis)

Uses chemical reagents at different concentrations to inhibit the different isoenzymes of ALP

A

Chemical Inhibition Test

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19
Q

Alkaline Phosphatase (Chemical Inhibition Test)

  1. Inhibits placental and intestinal ALP
  2. Inhibits liver and bone ALP

A. Levamisole
B. Synthetic or 3M Urea
C. Phenylalanine

A
  1. B and C
  2. A
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20
Q

Alkaline Phosphatase (Methods of Analysis)

  • The most specific method for ALP analysis (recommended by IFCC)
  • It measures however the total ALP amount and not the specific isoenzymes
  • It incorporates the concept of absolute specificity
  • A kinetic method that requires continuous monitoring at 405nm between a pH of 10 to 15
  • It reacts p-nitrophenylphosphate (PNPP) with ALP to produce p-nitrophenol and phosphate ions
A

Bowers and McComb (Szasz Modification)

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21
Q

Diagnostic Significance of Alkaline Phosphatase

In cases of obstructive jaundice, ALP secretion in what organ is increased which leads to an increase in the total ALP?

A

Liver

When subjected under electrophoresis, the liver isoenzyme band may be increased

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22
Q

Diagnostic Significance of Alkaline Phosphatase

In patients with Paget’s disease or osteotitis deformans, ALP secretion in what organ is increased?

A

Bone

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23
Q

Diagnostic Significance of Alkaline Phosphatase

Patients who have undergone blood transfusion and cardiopulmonary bypass may exhibit a transient (increase/decrease) in ALP which will return to normal after some time

A

Decrease

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24
Q

Diagnostic Significance of Alkaline Phosphatase

What ALP is increased in the ff. patients?
- Dialysis patients
- Patients with low bone mineral disease (BMD) of the hips
- Those with chronic kidney disease

A

B1x isoform (modified bone ALP)

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25
Q

Diagnostic Significance of Alkaline Phosphatase

A prolonged (increase/decrease) in ALP is seen in patients with hypophosphatasia

A

Decrease

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26
Q

Abnormal Forms of Alkaline Phosphatase

  • Seen in lung, breast, ovarian, and gynecological cancer
  • It is a co-migrator of bone ALP, wherein they are seen in the same place when subjected under electrophoresis
  • The most heat stable, surviving at 65ºC for 30 minutes
  • Is inhibited by phenylalanine
A

Regan ALP

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27
Q

Abnormal Forms of Alkaline Phosphatase

  • Seen in patients with adenocarcinoma of the pancreas and bile duct, and pleural cancer
  • A variant of Regan ALP
  • It is inhibited by L-leucine and phenylalanine
A

Nagao ALP

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28
Q

Abnormal Forms of Alkaline Phosphatase

  • Mirrors the placental ALP
  • Seen in serum and CSF specimens of patients with germ cell tumors
  • Determination of this is useful in differentiating pinealoma and germ cell tumor
A

Placental-like Alkaline Phosphatase (PLAP)

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29
Q

Abnormal Forms of Alkaline Phosphatase

Placental-like Alkaline Phosphatase (PLAP) is increased in patients with a (pinealoma/germ cell tumor)

A

Germ Cell Tumor

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30
Q

Major Clinical Enzymes: Phosphatases

  • Aka “Acid Orthophosphoric Monoester Phosphohydrolase”
  • Catalyzes the same reaction with ALP except that this is acid-loving
  • Is maintained at a pH of 5 to 6
  • Is mainly measured for male clinical chemistry, but not limited to it
A

Acid Phosphatase (ACP)

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31
Q

Acid Phosphatase (ACP)

An unknown specimen having ACP levels of greater than 50 U/L may be determined as having what fluid mixed in with the specimen?

A

Seminal fluid

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32
Q

Acid Phosphatase (ACP)

Arrange the tissue sources of ACP from most to least abundant:
- Platelets
- Liver
- Prostate gland
- RBCs
- Bones

A
  1. Prostate gland
  2. RBCs
  3. Platelets
  4. Liver
  5. Bones
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33
Q

Acid Phosphatase (ACP) Reference Values for Males

Determine if for Total ACP or Prostatic ACP:
1. 2.5 to 11.7 U/L
2. 0 to 3.5 ng/ml

A
  1. Total ACP
  2. Prostatic ACP
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34
Q

Acid Phosphatase (ACP) Specimen Considerations

  1. Sample should be free of hemolysis since it may lead to a falsely (increased/decreased) value of ACP as RBC can also be the source of the enzyme
  2. A/an (increase/decrease) in the levels of ACP is seen when the sample is left at room temperature for 1 to 2 hours
A
  1. Increased
  2. Decrease
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35
Q

Acid Phosphatase (ACP) Specimen Considerations

This serves as the specific substrate for a quantitative endpoint reaction

A

Thymolphthalein monophosphate

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36
Q

Acid Phosphatase (ACP) Specimen Considerations

This substance may also be used when using an enzymatic kinetic method which requires continuous monitoring

A

A-naphthyl phosphate

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37
Q

Acid Phosphatase (ACP) Specimen Considerations

If the sample won’t be assayed immediately, it may be subjected to the following:
1. (Freezing/Refrigeration)
2. Acidification to a pH lower than 6.5 to make it stable for (two/three) days at room temperature

A
  1. Freezing
  2. Two (2)
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38
Q

Acid Phosphatase (ACP) Specimen Considerations

These serve as inhibitors for prostatic ACP

A

20mmol of L-tartrate ions

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39
Q

Acid Phosphatase (ACP) Specimen Considerations

This serves as an inhibitor for RBC ACP

A

1mmol of cupric sulfate + 2% formaldehyde

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40
Q

Acid Phosphatase (ACP) Diagnostic Significance

ACP is mainly used in males for the detection of what?

Note: The number of ACP increases due to an increase in the number of cells when diagnosed with this

A

Prostatic adenocarcinoma

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41
Q

Acid Phosphatase (ACP) Diagnostic Significance

ACP levels fall (faster/slower) than the prostate specific antigen (PSA) in cases of surgical treatment

A

Faster

PSA is mainly concerned with immunology rather than CC

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42
Q

Acid Phosphatase (ACP) Diagnostic Significance

ACP determination is also useful for rape cases wherein vaginal washings are examined for seminal fluid ACP which can persist for up to how many days?

A

4 days

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43
Q

Acid Phosphatase (ACP) Diagnostic Significance

This is a form of ACP that is resistant to L-tartrate and a known inhibitor of prostatic ACP, which is seen in chronic and hairy cell leukemia

A

Tartrate Resistant Acid Phosphatase (TRAP)

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44
Q

Acid Phosphatase (ACP) Diagnostic Significance

Increased or Decreased ACP?
- Urinary tract obstruction
- Acute urinary retention
- Extensive prostatic massage
- Prostatic inflammation
- Infarction or Ischemia
- Prostatic manipulations (e.g. needle biopsy and cytoscopy)
- Prostatic carcinoma
- Breast, lung, and thyroid carcinoma
- Gaucher’s disease
- Niemann Pick disease
- Thrombocytopenia

A

Increased

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45
Q

Major Clinical Enzymes: Transferases/Transaminases

Aspartate and α-ketoacid reacts with this enzyme which will catalyze the transfer of an amino group to produce oxaloacetate and glutamate

A

Aspartate Aminotransferases or Serum Glutamic Oxaloacetic Transaminase (AST/SGOT)

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46
Q

Major Clinical Enzymes: AST/SGOT

What are the 3 major tissue sources of AST?

A
  1. Cardiac (major)
  2. Liver
  3. Skeletal (minor)

Other sources: Kidney, Pancreas, and RBCs

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47
Q

Major Clinical Enzymes: AST/SGOT

What is the reference value?

A

5 to 37 U/L

48
Q

Major Clinical Enzymes: AST/SGOT

What are the 2 isoenzymes?

A
  1. Cytoplasmic AST (more predominant)
  2. Mitochondrial AST
49
Q

AST/SGOT Methods of Analysis

  • This method maintains a pH of 7.5
  • It pairs AST with malate dehydrogenase (MD) to monitor changes in absorbance at 340nm
  • AST reacts with aspartate and a-ketoglutarate to produce oxaloacetate with NADH
  • Oxaloacetate will be acted upon by MD to produce malate and NAD
A

Karmen Method

50
Q

AST/SGOT Diagnostic Significance

AST is beneficial in the evaluation of (acute/chronic) myocardial infarction as well as hepatocellular disorders and skeletal muscle involvement

A

Acute

51
Q

AST/SGOT Diagnostic Significance

In cases of Acute MI, AST is a major enzyme used to determine the severity of the heart attack wherein AST levels should exhibit the following:

  1. A (rise/fall) in values within 6 to 8 hours after infarction
  2. A (peak/drop) at 24 hours after infarction
  3. A/an (increase/decrease) back to normal within 5 days after infarction
A
  1. Rise
  2. Peak
  3. Decrease
52
Q

AST/SGOT Diagnostic Significance

Match the ff. timeframes with the events during an Acute MI:

  1. A rise in value within (blank) after infarction
  2. A peak at (blank) after infarction
  3. A decrease back to normal within (blank) after infarction

A. 24 hours
B. 5 days
C. 6 to 8 hours

A
  1. C
  2. A
  3. B
53
Q

AST/SGOT Diagnostic Significance

As a physician, there are two things to be considered when diagnosing AMI:
1. Specificity of the (enzyme/substrate)
2. The (rise/fall)

A
  1. Enzyme
  2. Rise
54
Q

AST/SGOT Diagnostic Significance

TOF: AST is specific for diagnosing AMI

AMI: Acute Myocardial Infarction

A

False (it can be sourced from other organs)

55
Q

AST/SGOT Diagnostic Significance

TOF: Monitoring and waiting for the rise of AST during an emergency AMI case is beneficial

A

False (it takes 6 to 8 hours before levels start to increase, and time is key in diagnosing AMI, a life-threatening disease)

56
Q

AST/SGOT Diagnostic Significance

AST is also used in monitoring therapy for what kind of drugs which are able to increase AST levels 3x than the upper limits of the reference value?

A

Hepatotoxic drugs

57
Q

AST/SGOT Diagnostic Significance

Chronic disorders result to a significant (increase/decrease) in AST level

A

Increase

58
Q

Major Clinical Enzymes: Transferases/Transaminases

  • Alanine and α-ketoglutarate reacts with this enzyme to produce glutamate and pyruvate
  • Is significant in the evaluation of hepatic disorders
  • It can also be used to monitor the course of liver treatment and effects of drug therapy
A

Alanine Aminotransferase or Serum Glutamic Pyruvic Transaminase (ALT/SGPT)

59
Q

Major Clinical Enzymes: Transferases/Transaminases

Which among AST and ALT is a more specific and sensitive screening test for post transfusion hepatitis and occupational toxic exposure?

A

Alanine Aminotransferase or Serum Glutamic Pyruvic Transaminase (ALT/SGPT)

60
Q

ALT/SGPT Specimen Considerations

What 4 samples can be used for ALT analysis?

A
  1. Plasma
  2. Bile
  3. CSF
  4. Saliva
61
Q

ALT/SGPT Specimen Considerations

ALT analysis requires what coenzyme?

A

Pyridoxal phosphate (vitamin B6)

62
Q

ALT/SGPT Specimen Considerations

A hemolyzed specimen may falsely increase the levels of ALT up to how many times?

A

10x

63
Q

ALT/SGPT Specimen Considerations

What anticoagulant tube must not be used for ALT analysis considering that it inhibits the activity of the enzyme?

A

Heparin (green-top)

64
Q

ALT/SGPT Methods of Analysis

  • This method maintains a pH of 7.5 and is read at 340nm
  • This couples ALT with lactate dehydrogenase (LD) which produces pyruvate
  • Pyruvate when combined with NADH and an H ion will be acted upon by LD to produce lactate and NAD
A

Coupled Enzyme Reaction

65
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
Major organ is the HEART

A

AST/SGOT

66
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
Major organ is the LIVER

A

ALT/SGPT

67
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
Substrate is Aspartic a-ketoglutaric acid

A

AST/SGOT

68
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
Substrate is Alanine a-ketoglutaric acid

A

ALT/SGPT

69
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
End products are glutamic acid and oxaloacetic acid

A

AST/SGOT

70
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
End products are glutamic acid and pyruvic acid

A

ALT/SGPT

71
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
The color developer is 2,4 DNPH

A

BOTH

Note: The developer is for spectrophotometer

72
Q

Transferases & Transaminases (Comparison Table)

Identify if AST/SGOT or ALT/SGPT:
The color intensifier is 0.4N of NaOH

A

BOTH

73
Q

Transferases & Transaminases (Comparison)

Identify if AST/SGOT or ALT/SGPT:
Disease involves more of the muscle

A

AST/SGOT

74
Q

Transferases & Transaminases (Comparison)

Identify if AST/SGOT or ALT/SGPT:
Disease is more localized in the liver

A

ALT/SGPT

75
Q

Transferases & Transaminases (Comparison)

In viral hepatitis, both ALT and AST levels are elevated. In order to determine what enzyme to use, what ratio is needed?

A

De Ritis Ratio (ratio between ALT and AST)

76
Q

Transferases & Transaminases (Comparison)

If the De Ritis Ratio is greater than 1.0 which is commonly seen in acute hepatitis, what enzyme may be used?

A

ALT/SGPT

77
Q

Major Clinical Enzymes

  • Aka “Alpha-1-4 glucan-4-glucohydrolase”
  • It is a standalone enzyme that catalyzes a specific reaction
  • Starch and glycogen will be acted upon by this enzyme to produce a reducing sugar (glucose)
  • It is the smallest enzyme (MW: 50,000-55,000 Daltons) hence is freely filtered by the glomerulus
  • Also one of the earliest pancreatic markers
A

Amylase (AMS)

78
Q

Amylase (AMS)

What are the 2 major tissue sources?

A
  1. Acinar cells of the pancreas
  2. Salivary glands

Other sources: Adipose, Fallopian tubes, SI, and Skeletal muscles

79
Q

Amylase (AMS)

What are the 2 reference values?

A
  1. 60 to 180 Somogyi units per dL (SU/dL)
  2. 95 to 290 U/L
80
Q

Amylase (AMS)

What are the 2 isoenzymes?

A
  1. Salivary (S) type/ Ptyalin
  2. Pancreatic (P) type/ Amylopsin
81
Q

Amylase (AMS)

This isoenzyme is inhibited by wheat germ lectin

A

Salivary (S) type/ Ptyalin

82
Q

Amylase (AMS) Specimen Considerations

Give 3 interferences of AMS

A
  1. Heparin
  2. TAGs
  3. Wheat germ
83
Q

Amylase (AMS) Specimen Considerations

An increase in AMS activity will be solved by (diluting/concentrating) the specimen

A

Diluting

84
Q

Amylase (AMS) Specimen Considerations

A/an (increase/decrease) in AMS levels can be caused by the use of morphine and other opiates

A

Increase

85
Q

Amylase (AMS) Specimen Considerations

What is the general substrate used for AMS?

A

Starch

86
Q

Amylase (AMS) Methods of Analysis

  • The reference method reported in Somogyi units (SU)
  • Starch is broken down by AMS to produce glucose which will then be subjected to other glucose methods in order to be measured
  • Amount of glucose = amount of amylase
A

Saccharogenic

87
Q

Amylase (AMS) Methods of Analysis

This measures enzyme activity by the decrease in substrate concentration

A

Amyloclastic

88
Q

Amylase (AMS) Methods of Analysis

This measures enzyme activity by the increase of color intensity of a soluble dye-substrate solution

A

Chromogenic

89
Q

Amylase (AMS) Methods of Analysis

  • This is a kinetic method which requires a continuous monitoring technique
  • Amylase is coupled with a number of enzymes such as glucosidase, hexokinase, and G6PD
  • Maltopentose is acted upon by AMS to produce maltotriose and maltose
  • Maltotriose and maltose will be acted upon by glucosidase to produce 5-glucose which will be combined with ATP to be acted upon by hexokinase
  • 5-glucose-6-phosphate along with ADP will be combined with NAD to be acted upon by G6PD to produce 5,6-phosphogluconolactone
A

Coupled Enzyme

90
Q

Amylase (AMS) Methods of Analysis

This is used to determine the state of renal filtration, and as amylase is freely filtered in the glomeruli, using their ratio may determine the state of renal filtration

A

Creatinine (for the amylase/creatinine ratio)

91
Q

Amylase/Creatinine Ratio

What is the reference value?

A

1% to 4% (or 0.01 to 0.04)

92
Q

Amylase/Creatinine Ratio

For patients with acute pancreatitis, the ratio may reach what values?

A

4% to 15%

93
Q

An increase in the AMS levels might indicate a/an (increase/decrease) in the filtration on this enzyme, which is an indication of an impaired glomerular function

A

Increase

94
Q

Amylase (AMS) Diagnostic Significance

AMS determination is useful in the evaluation of acute pancreatitis and parotitis since it can also be sourced from where?

A

Salivary glands

95
Q

Amylase (AMS) Diagnostic Significance

In cases of both pancreatitis and parotitis, an increase in plasma AMS may be seen along with an increase of AMS in the urine for up to how many days?

A

7 days

96
Q

Amylase (AMS) Diagnostic Significance

AMS may be used to evaluate the presence and/or severity of acute pancreatitis wherein the levels of the enzyme may exhibit the following:

  1. A (rise/fall) in 2 to 12 hours
  2. A (peak/drop) in 24 hours
  3. A/an (decrease/increase) back to normal levels in 3 to 5 days
A
  1. Rise
  2. Peak
  3. Decrease
97
Q

Amylase (AMS) Diagnostic Significance

Match the ff. timeframes with the events during acute pancreatitis:

  1. A rise in value within (blank)
  2. A peak at (blank)
  3. A decrease back to normal within (blank)

A. 2 to 12 hours
B. 24 hours
C. 3 to 5 days

A
  1. A
  2. B
  3. C
98
Q

Amylase (AMS) Diagnostic Significance

TOF: In cases of renal failure, an increase in AMS plasma will be seen along with a decrease of AMS in the urine

A

True

99
Q

Amylase (AMS) Diagnostic Significance

This is a form of amylase combined with an immunoglobulin, wherein it cannot be filtered by the glomerulus due to its larger size

A

Macroamylasemia

100
Q

Amylase (AMS) Diagnostic Significance

Increased or Decreased Amylase?
- Acute pancreatitis
- Ectopic pregnancy
- Peptic ulcer
- Alcoholism
- Mumps

A

Increased

101
Q

Major Clinical Enzymes

  • Aka “Triacylglycerol acylhydrolase”
  • It catalyzes the degradation of fats and triacylglycerols (TAG) which will result to the formation of alcohol with fatty acids, and 2-monoglyceride intermediates with fatty acids, respectively
  • It hydrolyzes the ester linkages of fats
A

Lipase (LPS)

102
Q

Lipase (LPS)

Lipase is the most specific pancreatic marker however one disadvantage is that?

A

It is a LATE pancreatic marker

103
Q

Lipase (LPS)

What is the major tissue source of lipase?

A

Pancreas

104
Q

Lipase (LPS)

What is the reference value?

A

Between 0 to 1 U/mL

105
Q

Lipase (LPS) Specimen Considerations

What is the main substrate?

A

Olive oil (Triolein)

Note: It is the purest form of TAG

106
Q

Lipase (LPS) Specimen Considerations

What is the coenzyme needed for the reaction to work?

A

Colipase (secreted by the pancreas together with bile salts)

107
Q

Lipase (LPS) Specimen Considerations

Lipase is inhibited by what component from red blood cells?

A

Hemoglobin

108
Q

Lipase (LPS) Methods of Analysis

The most commonly used method of analysis however it does not use 50% olive oil

A

Peroxidase Coupling

109
Q

Lipase (LPS) Methods of Analysis

  • The reference method for LPS analysis
  • Involves the hydrolysis of olive oil after 24 hours at 37 ºC and the titration of fatty acids using NaOH
  • The end product is fatty acids
  • The application of titration makes the method less efficient since it can be time-consuming and labor-intensive
A

Cherry Crandal Method

110
Q

Lipase (LPS) Methods of Analysis

What are the 3 methods of analysis?

A
  1. Peroxidase Coupling
  2. Tietz and Fiereck
  3. Cherry Crandal Method
111
Q

Lipase (LPS) Diagnostic Significance

In cases of chronic pancreatitis, acinar cell degradation is exhibited resulting to a/an (increase/decrease) in amylase along with lipase production

A

Decrease

112
Q

Lipase (LPS) Diagnostic Significance

Determination of LPS may also be used in diagnosing the presence and/or severity of acute pancreatitis. Wherein the LPS levels will exhibit the following:

  1. A (rise/fall) in 6 hours
  2. A (peak/drop) in 24 hours
  3. A/an (increase/decrease) to normal levels in 8 to 14 days
A
  1. Rise
  2. Peak
  3. Decrease
113
Q

Lipase (LPS) Diagnostic Significance

Match the ff. timeframes with the events during acute pancreatitis:

  1. A rise in value within (blank)
  2. A peak at (blank)
  3. A decrease back to normal within (blank)

A. 24 hours
B. 6 hours
C. 8 to 14 days

A
  1. B
  2. A
  3. C
114
Q

What are the 5 function markers of the pancreas?

A
  1. Amylase
  2. Lipase
  3. Trypsin
  4. Chymotrypsin
  5. Elastase-1
115
Q

Familiarize with the Amylase/Creatinine Ratio Formula

A

(urine amylase/serum amylase) x (serum creatinine/urine creatinine) x 100

Clinical Chemistry (CC 1) (33 decks)

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