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Journal of Protein Chemistry

, Volume 15, Issue 4, pp 345–350 | Cite as

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

  • Qing-Xi Chen
  • Wei Zhang
  • Wen-Zhu Zheng
  • Hong Zhao
  • Si-Xu Yan
  • Hong-Rui Wang
  • Hai-Meng Zhou
Article

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.

Key words

Alkaline phosphatase inhibition chemical modification N-bromosuccinimide 

Abbreviations

ALP

alkaline phosphatase

PNPP

p-nitrophenyl phosphate

NBS

N-bromosuccinimide

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References

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Copyright information

© Plenum Publishing Corporation 1996

Authors and Affiliations

  • Qing-Xi Chen
    • 1
  • Wei Zhang
    • 1
  • Wen-Zhu Zheng
    • 1
  • Hong Zhao
    • 1
  • Si-Xu Yan
    • 1
  • Hong-Rui Wang
    • 2
  • Hai-Meng Zhou
    • 2
  1. 1.Department of BiologyXiamen UniversityXiamenChina
  2. 2.Department of Biological Science and BiotechnologyTsinghua UniversityBeijingChina

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