Enzymes (part two) Flashcards

(65 cards)

1
Q

What are the 5 major liver enzymes

A
  1. Aspartate aminotransferase
  2. Alanine aminotrasferase
  3. Alkaline phosphatase
  4. Gamma-glutamyl transerase
  5. Cholinesterase
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2
Q
Aspartate Amiontransferase (AST) 
- Three biological sources
A
  1. Heart
  2. Skeletal Muscle
  3. Liver
    (4. Kidney)
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3
Q
Aspartate Amiontransferase (AST) 
- typical appearance, peak, and return to normal after myocardial infarction
A

Rises within 12 hours after onset of chest pain; peaks at 18-24 hours; normal within 4-5 days

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4
Q
Aspartate Amiontransferase (AST)
-Two liver diseases that give rise to the greatest elevations
A

Liver (hepatocellular) Disease

  1. Viral Hepatitis
  2. Liver carcinoma
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5
Q
Aspartate Amiontransferase (AST) 
- One muscular disease in which AST is elevated
A
  • Skelatal Muscle Disease (Muscular Dystrophy)
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6
Q
Aspartate Amiontransferase (AST) 
-If hemolyzed specimens are unacceptable
A

UNACCEPTABLE

-due to high intracellular concentration of AST

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7
Q

Principle biological source of ALT

A

Liver

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8
Q
alanine aminotransferase (ALT)
-relative use in the diagnosis of liver disease, compared to AST
A

useful in the diagnosis of acute and chronic liver disease; parallels the rise in AST activity

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9
Q
alanine aminotransferase (ALT)
-liver diseases in which it is elevated
A

ALT higher and persists longer than AST in hepatitis

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10
Q
alanine aminotransferase (ALT)
-Hemolysis acceptibility?
A

NO HEMOLYSIS

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11
Q
Alkaline Phosphatase (ALP) 
- four principal biological sources of total ALP
A

liver, bone, intestine, placenta

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12
Q
Alkaline Phosphatase (ALP) 
- Hepatobiliary diseases in which ALP is increased
A

biliary obstruction, hepatitis, cirrhosis, infectious mono, and metastic carcinoma

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13
Q
Alkaline Phosphatase (ALP)
- The hepatobiliary disease which gives rise to ALP's highest elevations
A

Biliary Obstruction

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14
Q
Alkaline Phosphatase (ALP) 
- Bone diseases in which ALP is increased
A

Bone tumors, Paget’s Disease, Rickets, osteomalacia, hyperparathyroidism, and healing fractures

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15
Q
Alkaline Phosphatase (ALP)
- Two bone diseases which tie rise to ALP's highest elevations
A

Bone tumors and Paget’s Disease

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16
Q
Alkaline Phosphatase (ALP) 
- If hemolyzed specimens are unacceptable
A

Gross hemolysis NOT acceptable (slight ok but must be documented)

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17
Q
Alkaline Phosphatase (ALP)
- Principle of the Bowers and McComb procedure using p-nitrophenylphosphate
A

reference method; kinetic method that uses pNPP as substrate and measures the rate of p-nitrophenoxide release in AMP buffer

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18
Q

Which specific isoenzymes may be distinguished using the heat stability, urea denaturation, amino acid inhibition, and electrophoretic techniques

A

Alkaline Phosphatase (ALP)

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19
Q
Alkaline Phosphatase (ALP)
- Why the reference range is higher in children than in adults
A

due to rapid bone growth

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20
Q

gamma-glutamyltransferase (GGT)

-two principle biological sources

A

primarily liver, also kidney

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21
Q

gamma-glutamyltransferase (GGT)

-degree of elevation used in the differential diagnosis of hepatocellular VS biliary tract disease

A

Elevation up to 5X ULN in biliary tract disorders; lesser elevation (2-5X) in viral hepatitis or active cirrhosis

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22
Q

gamma-glutamyltransferase (GGT)

-clinical usefulness in the diagnosis and monitoring of chronic alcoholism

A

GGT is induced by alcohol and other drugs; used as a marker to check for abstinence from alcohol

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23
Q

cholinesterase (ChE) in vivo reaction it catalyzes

A

Both enzymes hydrolyze choline esters to form choline and the corresponding fatty acid at the neuromuscular junction

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24
Q

Three clinical applications of measuring ChE activity

A

1 assess exposure to organophospahtes found in insecticides and nerve gas
2 check how patient will react to general anesthesia
3 assess presence of cirrhosis, hepatitis, liver carcinoma (due to decreased production)

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25
Sources of AChE (acetylcholinesterase)
Red blood cells and central nervous system
26
Sources of cholinesterase (ChE)
Liver, white matter of brain, serum
27
``` creatine kinase (CK) -in vivo reaction it catalyzes ```
Catalysis for ATP formation and phosphorylation of creatine in energy production or usage
28
``` Creatine Kinase (CK) -three principle tissue sources ```
skeletal and cardiac muscle, brain
29
``` Creatine Kinase (CK) -dimeric composisition and sources of its three isoenzymesm ```
composed of two subunits (M and B); Isoenzymes formed: CK-MM, CK-MB, CK-BB
30
``` Creatine Kinase (CK) -typical apprearance, peak, and return to normal after a myocardial infarction ```
Rises 3-8 hours after the onset of chest pain (1st to rise) Activity peaks at 10-36 hours Levels return to normal in 3-4 Days
31
``` Creatine Kinase (CK) -one muscular disease that gives rise to CK's highest elevations ```
Duchenne's Muscular Dystrophy (50X ULN)
32
``` Creatine Kinase (CK) -cerebral diseases in which CK is elevated ```
Cerebral vascular accident (CVA), stroke, cerebral ischemia
33
``` Creatine Kinase (CK) -principle of the Oliver and Rosalki method ```
Analytical procedure for total CK; Increase in absorbance as NADP is oxidized is measured at 340 nm
34
Lipase (LPS) | -principle biological source
Pancreas
35
Lipase (LPS) | -two diseases in which LPS is elevated
Acute pancreatitis and chronic pancreatitis
36
Lipase (LPS) | -a comparison between the usefulness of LPS and AMS measurements in the diagnosis of pancreatitis
levels parallel AMS appearance, but LPS is more specific than AMS
37
Lipase (LPS) | -principles of the turbidimetric/nephelometric procedures
Olive oil emulsion is hydrolyzed by LPS, causing a DECREASE in turbidimetry
38
Lipase (LPS) | -principle of coupled enzymatic analytical procedure
LPS hydrolyzes fatty acids to form free glycerol which is quantitated colorimetrically
39
Clinical usefulness of performing acid phosphatase (ACP) measurements
used to diagnose diseases of the prostate; can also do a prostatic acid phosphatase (PAP) and PSA
40
Glucose-6-phosphate dehydrogenase (G-6-PD) | -biological sources
RED BLOOD CELLS, adrenal cortex, lymph nodes, thymus, spleen
41
Glucose-6-phosphate dehydrogenase (G-6-PD) | -disease state associated with LOW levels of G-6-PD
hemolytic anemia
42
four major coenzymes used in electron transfer reactions commonly employed in enzyme assays in the lab, including specific wavelength for measurement
NAD, NADH, NADP, NADPH; wavelength 340
43
Clinically significant enzymes/lab findings | -myocardial infarction
I CK, I CKMB, I AST, I LD
44
Clinically significant enzymes/lab findings | -liver (hepatocellular) disease
AST and ALT
45
Clinically significant enzymes/lab findings | -Liver (hepatobiliary) disease
ALP and GGT
46
Clinically significant enzymes/lab findings | -bone disease
ALP
47
Clinically significant enzymes/lab findings | -brain disease
CK-BB, CK
48
Clinically significant enzymes/lab findings | -prostate cancer and hypertrophy
ACP
49
Clinically significant enzymes/lab findings | -acute and chronic pancreatitis
LPS AMS
50
Clinically significant enzymes/lab findings | -muscle disease and muscular dystrophy
CK-MM CK ALS
51
``` Lactate Dehydronase (LD) - seven principle biological sources ```
Ubiquitous! 1. Brain 2. RBCs 3. WBCs 4. Kidney 5. Liver 6. Lung 7. Cardiac 8. Skeletal muscle
52
``` Lactate Dehydronase (LD) -after myocardial infarction ```
- 10X increase above UNL - increase 8-18 hours after onset of chest pain - peaks 48-72 hours - returns normal 6-10 days - ELP shows LD1 > LD 2 or "flipped pattern"
53
``` Lactate Dehydronase (LD) -liver disease which it is elevated ```
Hepatobiliary disease
54
``` Lactate Dehydronase (LD) - liver disease that gives rise to the greatest elevation ```
Metastatic cancer
55
``` Lactate Dehydronase (LD) - two types of anemia where it is elevated ```
Megaloblastic anemia | Pernicious anemia
56
``` Lactate Dehydronase (LD) -hemolysis acceptable? ```
Acceptable, but make a comment. Hemolysis increases LD in vivo, and in vitro.
57
Aldolase (ALS) | - three principle biological sources
- skeletal - muscle - brain
58
Aldolase (ALS) | -one disease state where it is elevated
Skeletal muscle diseases, such as muscular dystrophy
59
Amylase (AMS) | - two principle biological sources
1. Pancreas 2. Salivary glands 3. Macroamylase
60
Amylase (AMS) | - clinical significance of macroamylase
AMS bound to IgG or IgA, causing an increase in total AMS without apparent disease
61
Amylase (AMS) | - clinical significance of measurements in diagnosis of acute pancreatitis, chronic pancreatitis, and mumps
???
62
Amylase (AMS) | - what method measures amount of sugars formed from hydrolytic activity of AMS
Saccharogenic
63
Amylase (AMS) | - what method uses dye-labeled starch substrates; as AMS hydrolyzes the starch, an increase in color is quantified
Chromilytic
64
Amylase (AMS) | -method that measures decrease in starch substrate concentration as AMS works on starch.
Amyloclastic Assays
65
Amylase (AMS) | -method that is a glucose coupled reaction and a hexokinase coupled reaction
Enzymatic Assays