Quantitative Determination Of Aspartate Aminotransferase GOT (AST)
Commentaire de texte : Quantitative Determination Of Aspartate Aminotransferase GOT (AST). Recherche parmi 300 000+ dissertationsPar yass111 • 16 Novembre 2014 • Commentaire de texte • 270 Mots (2 Pages) • 613 Vues
Quantitative determination of aspartate aminotransferase
GOT (AST)
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PRINCIPLE OF THE METHOD
Aspartate aminotransferase (AST) formerly called glutamate oxaloacetate
(GOT) catalyses the reversible transfer of an amino group from aspartate
to -ketoglutarate forming glutamate and oxalacetate. The oxalacetate
produced is reduced to malate by malate dehydrogenase (MDH) and
NADH:
L-Aspartate + -Ketoglutarate
AST
Glutamate + Oxalacetate
Oxalacetate + NADH + H
+
MDH
Malate + NAD
+
The rate of decrease in concentration of NADH, measured photometrically,
is proportional to the catalytic concentration of AST present in the sample
1
.
CLINICAL SIGNIFICANCE
The AST is a cellular enzyme, is found in highest concentration in heart
muscle, the cells of the liver, the cells of the skeletal muscle and in smaller
amounts in other weaves.
Although an elevated level of AST in the serum is not specific of the
hepatic disease, is used mainly to diagnostic and to verify the course of
this disease with other enzymes like ALT and ALP.
Also it is used to control the patients after myocardial infarction, in skeletal
muscle disease and other
1,4,5
.
Clinical diagnosis should not be made on a single test result; it should
integrate clinical and other laboratory data.
...