Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosnccinimide

被引:35
作者
Chen, QX
Zhang, W
Zheng, WZ
Zhao, H
Yan, SX
Wang, HR
Zhou, HM
机构
[1] TSING HUA UNIV,DEPT BIOL SCI & BIOTECHNOL,BEIJING 100084,PEOPLES R CHINA
[2] XIAMEN UNIV,DEPT BIOL,XIAMEN 361005,PEOPLES R CHINA
来源
JOURNAL OF PROTEIN CHEMISTRY | 1996年 / 15卷 / 04期
关键词
alkaline phosphatase; inhibition; chemical modification; N-bromosuccinimide;
D O I
10.1007/BF01886860
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
The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mol. Biol. 61, 381-436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
引用
收藏
页码:345 / 350
页数:6
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