Enzymes (part two) Flashcards
What are the 5 major liver enzymes
- Aspartate aminotransferase
- Alanine aminotrasferase
- Alkaline phosphatase
- Gamma-glutamyl transerase
- Cholinesterase
Aspartate Amiontransferase (AST) - Three biological sources
- Heart
- Skeletal Muscle
- Liver
(4. Kidney)
Aspartate Amiontransferase (AST) - typical appearance, peak, and return to normal after myocardial infarction
Rises within 12 hours after onset of chest pain; peaks at 18-24 hours; normal within 4-5 days
Aspartate Amiontransferase (AST) -Two liver diseases that give rise to the greatest elevations
Liver (hepatocellular) Disease
- Viral Hepatitis
- Liver carcinoma
Aspartate Amiontransferase (AST) - One muscular disease in which AST is elevated
- Skelatal Muscle Disease (Muscular Dystrophy)
Aspartate Amiontransferase (AST) -If hemolyzed specimens are unacceptable
UNACCEPTABLE
-due to high intracellular concentration of AST
Principle biological source of ALT
Liver
alanine aminotransferase (ALT) -relative use in the diagnosis of liver disease, compared to AST
useful in the diagnosis of acute and chronic liver disease; parallels the rise in AST activity
alanine aminotransferase (ALT) -liver diseases in which it is elevated
ALT higher and persists longer than AST in hepatitis
alanine aminotransferase (ALT) -Hemolysis acceptibility?
NO HEMOLYSIS
Alkaline Phosphatase (ALP) - four principal biological sources of total ALP
liver, bone, intestine, placenta
Alkaline Phosphatase (ALP) - Hepatobiliary diseases in which ALP is increased
biliary obstruction, hepatitis, cirrhosis, infectious mono, and metastic carcinoma
Alkaline Phosphatase (ALP) - The hepatobiliary disease which gives rise to ALP's highest elevations
Biliary Obstruction
Alkaline Phosphatase (ALP) - Bone diseases in which ALP is increased
Bone tumors, Paget’s Disease, Rickets, osteomalacia, hyperparathyroidism, and healing fractures
Alkaline Phosphatase (ALP) - Two bone diseases which tie rise to ALP's highest elevations
Bone tumors and Paget’s Disease
Alkaline Phosphatase (ALP) - If hemolyzed specimens are unacceptable
Gross hemolysis NOT acceptable (slight ok but must be documented)
Alkaline Phosphatase (ALP) - Principle of the Bowers and McComb procedure using p-nitrophenylphosphate
reference method; kinetic method that uses pNPP as substrate and measures the rate of p-nitrophenoxide release in AMP buffer
Which specific isoenzymes may be distinguished using the heat stability, urea denaturation, amino acid inhibition, and electrophoretic techniques
Alkaline Phosphatase (ALP)
Alkaline Phosphatase (ALP) - Why the reference range is higher in children than in adults
due to rapid bone growth
gamma-glutamyltransferase (GGT)
-two principle biological sources
primarily liver, also kidney
gamma-glutamyltransferase (GGT)
-degree of elevation used in the differential diagnosis of hepatocellular VS biliary tract disease
Elevation up to 5X ULN in biliary tract disorders; lesser elevation (2-5X) in viral hepatitis or active cirrhosis
gamma-glutamyltransferase (GGT)
-clinical usefulness in the diagnosis and monitoring of chronic alcoholism
GGT is induced by alcohol and other drugs; used as a marker to check for abstinence from alcohol
cholinesterase (ChE) in vivo reaction it catalyzes
Both enzymes hydrolyze choline esters to form choline and the corresponding fatty acid at the neuromuscular junction
Three clinical applications of measuring ChE activity
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)
Sources of AChE (acetylcholinesterase)
Red blood cells and central nervous system
Sources of cholinesterase (ChE)
Liver, white matter of brain, serum
creatine kinase (CK) -in vivo reaction it catalyzes
Catalysis for ATP formation and phosphorylation of creatine in energy production or usage
Creatine Kinase (CK) -three principle tissue sources
skeletal and cardiac muscle, brain
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
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
Creatine Kinase (CK) -one muscular disease that gives rise to CK's highest elevations
Duchenne’s Muscular Dystrophy (50X ULN)
Creatine Kinase (CK) -cerebral diseases in which CK is elevated
Cerebral vascular accident (CVA), stroke, cerebral ischemia
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
Lipase (LPS)
-principle biological source
Pancreas
Lipase (LPS)
-two diseases in which LPS is elevated
Acute pancreatitis and chronic pancreatitis
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
Lipase (LPS)
-principles of the turbidimetric/nephelometric procedures
Olive oil emulsion is hydrolyzed by LPS, causing a DECREASE in turbidimetry
Lipase (LPS)
-principle of coupled enzymatic analytical procedure
LPS hydrolyzes fatty acids to form free glycerol which is quantitated colorimetrically
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
Glucose-6-phosphate dehydrogenase (G-6-PD)
-biological sources
RED BLOOD CELLS, adrenal cortex, lymph nodes, thymus, spleen
Glucose-6-phosphate dehydrogenase (G-6-PD)
-disease state associated with LOW levels of G-6-PD
hemolytic anemia
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
Clinically significant enzymes/lab findings
-myocardial infarction
I CK, I CKMB, I AST, I LD
Clinically significant enzymes/lab findings
-liver (hepatocellular) disease
AST and ALT
Clinically significant enzymes/lab findings
-Liver (hepatobiliary) disease
ALP and GGT
Clinically significant enzymes/lab findings
-bone disease
ALP
Clinically significant enzymes/lab findings
-brain disease
CK-BB, CK
Clinically significant enzymes/lab findings
-prostate cancer and hypertrophy
ACP
Clinically significant enzymes/lab findings
-acute and chronic pancreatitis
LPS AMS
Clinically significant enzymes/lab findings
-muscle disease and muscular dystrophy
CK-MM CK ALS
Lactate Dehydronase (LD) - seven principle biological sources
Ubiquitous!
- Brain
- RBCs
- WBCs
- Kidney
- Liver
- Lung
- Cardiac
- Skeletal muscle
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”
Lactate Dehydronase (LD) -liver disease which it is elevated
Hepatobiliary disease
Lactate Dehydronase (LD) - liver disease that gives rise to the greatest elevation
Metastatic cancer
Lactate Dehydronase (LD) - two types of anemia where it is elevated
Megaloblastic anemia
Pernicious anemia
Lactate Dehydronase (LD) -hemolysis acceptable?
Acceptable, but make a comment. Hemolysis increases LD in vivo, and in vitro.
Aldolase (ALS)
- three principle biological sources
- skeletal
- muscle
- brain
Aldolase (ALS)
-one disease state where it is elevated
Skeletal muscle diseases, such as muscular dystrophy
Amylase (AMS)
- two principle biological sources
- Pancreas
- Salivary glands
- Macroamylase
Amylase (AMS)
- clinical significance of macroamylase
AMS bound to IgG or IgA, causing an increase in total AMS without apparent disease
Amylase (AMS)
- clinical significance of measurements in diagnosis of acute pancreatitis, chronic pancreatitis, and mumps
???
Amylase (AMS)
- what method measures amount of sugars formed from hydrolytic activity of AMS
Saccharogenic
Amylase (AMS)
- what method uses dye-labeled starch substrates; as AMS hydrolyzes the starch, an increase in color is quantified
Chromilytic
Amylase (AMS)
-method that measures decrease in starch substrate concentration as AMS works on starch.
Amyloclastic Assays
Amylase (AMS)
-method that is a glucose coupled reaction and a hexokinase coupled reaction
Enzymatic Assays