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