|
type |
Journal Article |
authors |
Yamaguchi, T.; Matsumura, Y. |
title |
Purification of L-glutamate decarboxylase by affinity chromatography |
journal |
Biochim Biophys Acta |
Activity |
4.1.1.15 |
ui |
77158018 |
year |
(1977) |
volume |
481 |
number |
2 |
pages |
706-11. |
| |
keywords |
Animal |
abstract |
L-Glutamate decarboxylase (L-glutamate 1-carboxy-lyase, EC 4.1.1.15) from rat brain synaptosomal extract was partially purified by affinity chromatography. On further purification by DEAE-Sephadex A 50 and Sephadex G-200, L-glutamate decarboxylase was purified to greater extent. It was found that a single affinity chromatography by appropriate elution gave a highly purified protein giving a single band of high specific activity on polyacrylamide gradient gel slab electrophoresis with minimal contamination. Substrate specificity of the purified enzyme was modified in the presence of 6-azauracil or phenylalanine resulting in decreased specificity to L-glutamate and increased specificity to L-aspartate. |
last changed |
2002/11/12 16:17 |
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