POSSIBLE INVOLVEMENT OF MANGANESE IN THE CATALYTIC MECHANISM OF BOVINE LIVER ARGINASE

被引：14

作者：

TURKOGLU, S ^{[1
]}

OZER, I ^{[1
]}

机构：

[1] HACETTEPE UNIV,SCH PHARM,DEPT BIOCHEM,ANKARA,TURKEY

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1992年 / 24卷 / 06期

关键词：

D O I：

10.1016/0020-711X(92)90100-F

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：

1. Bovine liver arginase followed Michaelis-Menten kinetics in the pH range of 4.5-9.0. The variation of upsilon(i) pH implied that a basic group (pK(alpha) 8.7) functions at the catalytic site. 2. Treatment of the enzyme with N-ethylmaleimide showed that there are no critical sulfhydryl groups on the enzyme. 3. The less selective reagent, 3-bromopyruvate, caused biphasic inactivation which was unaffected by the presence of ornithine. 4. The data pointed against critical involvement of active site amino acid side chains in the catalytic sequence in arginase. 5. The observed pH-rate profile may reflect ionization of metal-bound water.

引用

页码：937 / 939

页数：3

共 19 条

[1] EFFECT OF NADH ON THE PKA OF ZINC-BOUND WATER IN LIVER ALCOHOL-DEHYDROGENASE [J].