|
type |
Journal Article |
authors |
Noguchi, T.; Takada, Y.; Kido, R. |
title |
Glutamate-glyoxylate aminotransferase in rat liver cytosol. Purification, properties and identity with alanine-2-oxoglutarate aminotransferase |
journal |
Hoppe Seylers Z Physiol Chem |
Activity |
2.6.1.4 |
sel |
selected |
ui |
590935 |
year |
(1977) |
volume |
358 |
number |
12 |
pages |
1533-42 |
| |
keywords |
Alanine Transaminase/*metabolism |
abstract |
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. |
last changed |
2009/03/24 16:15 |
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