|
type |
Journal Article |
authors |
Harada I, Noguchi T, Kido R.
|
title |
Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver
|
journal |
Hoppe Seylers Z Physiol Chem. |
Activity |
2.6.1.60 |
sel |
selected |
ui |
25837 b |
year |
(1978) |
volume |
359 |
number |
4 |
pages |
481-8 |
| |
keywords |
Animal |
abstract |
Aromatic-amino-acid-glyoxylate aminotransferase was highly purified from the mitochondrial fraction of livers from monkey and glucagon-injected rats. The two enzyme preparations showed physical and enzymic properties different from a kynurenine aminotransferase previously described. The two enzymes had nearly identical molecular weights (approximate 80 000), isoelectric points (pH 8.0) and pH optima (pH 8.0 - 8.5). However, a difference in substrate specificity was observed between the two enzymes. Both enzymes utilized glyoxylate, pyruvate, hydroxypyruvate and 2-oxo-4-methyl-thiobutyrate as effective amino acceptors. 2-Oxoglutarate was active for rat enzyme but not for monkey enzyme. With glyoxylate, amino donors were effective in the following order of activity; phenylalanine greater than histidine greater than tyrosine greater than tryptophan greater than 5-hydroxytrypotphan greater than kynurenine for the rat enzyme, and phenylalanine greater than kynurenine greater than histidine greater than tryptophan greater than 5-hydroxy-tryptophan for the monkey enzyme. |
last changed |
2009/01/08 15:49 |
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