Glutamic oxalacetic transaminase (GOT, aspartate aminotransferase EC 2.6.1.1) catalyzes reversibly the transamination of the amino, -NH2, group of L-aspartic acid to a- letoglutaric acid with the subsequent formation of oxalacetic acid and L-glutamic acid, respectively. Detection of the enzyme activity in blood serum is used for clinical diagnosis of myocardial infraction, hepatitis and other diseases. Therefore, the availability of sensitive, accurate and reproducible methods for the assay of GOT activity is of prime clinical importance. The research proposes the development of new analytical method in which both spectrophotometeic and potentiometric techniques will be applied for the assay of GOT activity in flow-injection system for clinical purposes. L-aspartate produced during the more favorable GOT catalyzed reaction can be converted to ammonium ion and funarate in the presence of L-aspartase. The ammonium ion, subsequently, can be detected spectrophotometrically and potentiometrically using ammonium ion selective electrodes. The concentration of ammonium ion is directly related to GOT activity. The application of two electrodes of the same kind; as reference and indicating electrodes; in flow system increases the sensitivity and minimizes interferences. The suggested methods are specific, accurate and sensitive. The proposed research also provide means and valuable information for kinetic studies of the GOT enzyme system.
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