SUMMARY: Cell-free extracts of trophozoites of Hartmannella (Culbertson strain a-i), grown axenically, catalysed transamination between 2-oxoglutarate and a number of amino acids. Aspartic acid, alanine and serine showed the maximum activity. The L-alanine-2-oxoglutarate aminotransferase (E.C. was purified about 15-fold by adsorption with calcium phosphate gel and elution with 0-2 M-phosphate buffer. Stability during storage, pH optima in different buffers values for alanine and 2-oxoglutarate, and the role of pyridoxal-5-phosphate are reported. -Chloromercuribenzoate, cyanide and metal-chelating agents markedly inhibited the enzyme. Among dicarboxylic acids, maleic acid had the maximum inhibitory effect. Amoe-bicidal drugs and antibiotics had no marked inhibitory effect on the enzyme.


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