SOME PROPERTIES OF GLUTAMATE DEHYDROGENASE FROM PEA SEEDLINGS

被引：33

作者：

YAMASAKI, K

SUZUKI, Y

机构：

[1] Laboratory of Plant Physiology, Biological Institute, University of Toyama, Toyama

来源：

PHYTOCHEMISTRY | 1969年 / 8卷 / 06期

关键词：

D O I：

10.1016/S0031-9422(00)86338-4

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：

Glutamate: NAD oxidoreductase, deaminating (E.C. 1.4.1.2) was partially purified from pea seedlings. Optimum pHs for the reductive amination and oxidative deamination were 7·5 and 10·0 respectively. Michaelis constants were 1·6 × 10-3 M for glutamate and 4·1 × 10-5 M for NAD+. Activity was inhibited by p-chloromercuriphenylsulfonic acid (PCMPSA), phenylmercuric acetate, o-phenanthroline, ethylenediamine tetraacetate (EDTA), zincon and other metal-binding reagents. Inhibition by PCMPSA was reversed by reduced glutathione. Meanwhile, the activity was much decreased by dialysis against EDTA solution and its activity was restored by the addition of several divalent cations. © 1969.

引用

页码：963 / &

共 12 条

[1]

ADELSTEIN SJ, 1958, J BIOL CHEM, V233, P589

[2] THE ISOLATION AND CHARACTERIZATION OF GLUTAMIC DEHYDROGENASE FROM CORN LEAVES [J].