type	Journal Article
authors	Blindermann, J. M.; Maitre, M.; Ossola, L.; Mandel, P.
title	Purification and some properties of L-glutamate decarboxylase from human brain
journal	Eur J Biochem
Activity	4.1.1.15
ui	78190613
year	(1978)
volume	86
number	1
pages	143-52.
keywords	Amino Acids/analysis
abstract	Glutamate decarboxylase (EC 4.1.1.15) from human brain has been purified 8000-fold with respect to the initial homogenate. The molecular weight of the native enzyme was found to be 140000 by electrophoresis on a polyacrylamide gradient gel slab. The presence of a single protein band (Mr 67000) on sodium dodecylsulphate/polyacrylamide gel and the existence of only one N- terminal amino acid suggest that the enzyme consists of two similar if not identical polypeptide chains. The Km of the enzyme at the optimum pH of 6.8 is about 1.3 x 10(-3) M for glutamate and 0.13 x 10(-6) M for pyridoxal phosphate. The analysis of the effects of various inhibitors of mouse brain glutamate decarboxylase on the human enzyme confirms the strong competitive inhibition caused by 3-mercaptopropionic acid (Ki = 2.7 x 10(-6) M) while the Ki values for allylglycine and chloride ion are 1.8 x 10(-2) M and 2.2 x 10(-2) M, respectively.
last changed	2002/11/12 16:17