ALANINE AMINOTRANSFERASE (AST, SGOT) REAGENT (UV-KINETIC)
INTENDED USE
Aspartate Aminotransferase (AST, SGOT) Reagent (UV-Kinetic) is used for the quantitative determination of Aspartate Aminotransferase (AST) in human serum.
INTRODUCTION
Serum aspartate aminotransferase (AST) also known as serum glutamic oxalacetic transaminase (SGOT) is a tissue enzyme that catalyzes the exchange of amino and keto groups between alpha-amino acids and alpha-keto acids. AST is widely distributed in tissue principally cardiac, hepatic, muscle and kidney. Injury to these tissues results in the release of the AST (SGOT) enzyme to general circulation. Following a myocardial infarction, serum levels of AST (SGOT) are elevated and reach a peak 48 to 60 hours after onset. Hepatobiliary diseases, such as cirrhosis, metastatic carcinoma, and viral hepatitis also will increase serum AST levels. The first kinetic assay of AST for diagnostic purposes was described by Karmen et al. in 1955, using a coupled reaction of malate dehydrogenase (MDH) and NADH. This assay system was critically evaluated and optimized in 1960 by Henry et al. In 1977 the International Federation of Clinical Chemistry recommended a reference procedure for the measurement of AST activity based upon Karmen's procedures. The AST reagent applies the formulation recommended by the IFCC.
PRINCIPLE
Aspartate Aminotransferase (AST, SGOT) Reagent (UV-Kinetic)
AST catalyzes the transfer of an amino group between L-aspartate and 2-Oxoglutarate. The oxalacetate formed in the first reaction is then reacted with NADH in the presence of malate dehydrogenase (MDH) to form NAD. AST activity is determined by measuring the rate of oxidation of NADH at 340 nm. Lactate dehydrogenase is included in the reagent to convert endogenous pyruvate in the sample to lactate during the lag phase prior to measurement.
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