Glutamate-glyoxylate aminotransferase in rat liver cytosol. Purification, properties and identity with alanine-2-oxoglutarate aminotransferase.
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.
D000410:Alanine Transaminase / Q000378:metabolism*; D000818:Animals; D003348:Cortisone / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D005971:Glutamates; D006038:Glyoxylates; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats; D013379:Substrate Specificity; D000637:Transaminases / Q000302:isolation & purification / Q000378:metabolism*
D005971:Glutamates; D006038:Glyoxylates; D000637:Transaminases; D000410:Alanine Transaminase; D003348:Cortisone