PMID: 590935Dec 1, 1977

Glutamate-glyoxylate aminotransferase in rat liver cytosol. Purification, properties and identity with alanine-2-oxoglutarate aminotransferase

Hoppe-Seyler's Zeitschrift für physiologische Chemie
T NoguchiR Kido


After cortisone injection, virtually identical increases in rat liver cytosol alanine-2-oxoglutarate aminotransferase and glutamate-glyoxylate aminotransferase activities were observed. The two activities were co-purified to homogeneity from rat liver cytosol. The purified enzyme was specific for L-alanine with 2-oxoglutarate as amino acceptor. With glyoxylate, however, the enzyme utilized various L-amino acids as amino donors in the following order of activity: glutamate greater than alanine greater than glutamine greater than methionine. The ratio of alanine-2-oxoglutarate aminotransferase activity to glutamate-glyoxylate aminotransferase activity remained constant during purification and was unchanged by a variety of treatments of the purified enzyme. These results suggest that glutamate-glyoxylate aminotransferase is identical with alanine-2-oxoglutarate aminotransferase. Evidence was obtained that the two enzyme activities in the cytosol of dog, cat and human liver are also properties of the same protein.


Feb 11, 1970·Biochimica Et Biophysica Acta·Y NakataniK Higashino
Dec 1, 1964·Journal of Biochemistry·N KATUNUMAI TOMINO


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Apr 1, 1997·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·C J Danpure
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