PURIFICATION AND PROPERTIES OF RAT-BRAIN GLUTAMATE-DEHYDROGENASE

被引：77

作者：

CHEE, PY ^{[1
]}

DAHL, JL ^{[1
]}

FAHIEN, LA ^{[1
]}

机构：

[1] UNIV WISCONSIN,SCH MED,DEPT PHARMACOL,MADISON,WI 53706

来源：

JOURNAL OF NEUROCHEMISTRY | 1979年 / 33卷 / 01期

关键词：

D O I：

10.1111/j.1471-4159.1979.tb11705.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

—A method is described for the preparation of glutamate dehydrogenase in a highly purified form from rat brain. Only one protein band was detected when the enzyme was subjected to electrophoresis on SDS polyacrylamide gels. The rat brain enzyme was essentially identical to the rat liver enzyme with respect to electrophoresis on SDS polyacrylamide gels, immunochemical properties and most kinetic parameters. However, the brain enzyme was much less reactive with glutamate, was more sensitive to inhibition by haloperidol, and was considerably more stable than the liver enzyme. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：53 / &

共 29 条

[1] CRYSTALLIZATION AND SOME PROPERTIES OF GLUTAMATE DEHYDROGENASE FROM RAT LIVER [J].