Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide |
| |
Authors: | Qing-Xi Chen Wei Zhang Wen-Zhu Zheng Hong Zhao Si-Xu Yan Hong-Rui Wang and Hai-Meng Zhou |
| |
Institution: | (1) Department of Biology, Xiamen University, 361005 Xiamen, China;(2) Department of Biological Science and Biotechnology, Tsinghua University, 100084 Beijing, China |
| |
Abstract: | 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.Abbreviations ALP
alkaline phosphatase
- PNPP
p-nitrophenyl phosphate
- NBS
N-bromosuccinimide |
| |
Keywords: | Alkaline phosphatase inhibition chemical modification N-bromosuccinimide |
本文献已被 SpringerLink 等数据库收录! |