Abstract
This chapter provides an overview of taurine–glutamate transaminase. Taurine:α-ketoglutrate aminotransferase catalyzes the transamination of taurine with α-ketoglutarate to yield sulfoacetaldehyde and L-glutamate, and the reverse reaction. The assay method is based on the measurement of glutamate or sulfoacetaldehyde. Glutamate is determined with ninhydrin after the separation by circular paper chromatography. Sulfoacetaldehyde is determined by the reaction with 2,4-dinitrophenylhydrazine, or o-aminobenzaldehyde in the presence of glycine. The purification procedure consists of several steps including preparation of crude extract, diethylaminoethyl (DEAE)-cellulose column chromatography, first sephadex G-150 column chromatography, hydroxylapatite column chromatography, and ammonium sulfate fractionation. The crystalline enzyme is homogeneous by the criteria of ultracentrifugation and disc gel electrophoresis. The sedimentation coefficient of the enzyme is determined to be 9.1 S. The taurine transaminase activity is found only in the extracts of Achromobacter superficialis ICR B-89 and Achromobacter polymorph ICR B-88. The enzyme activity is induced by β-alanine, but not by taurine.
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