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.
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Abbreviations
- ALP:
-
alkaline phosphatase
- PNPP:
-
p-nitrophenyl phosphate
- NBS:
-
N-bromosuccinimide
References
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Chen, QX., Zhang, W., Zheng, WZ. et al. Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide. J Protein Chem 15, 345–350 (1996). https://doi.org/10.1007/BF01886860
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DOI: https://doi.org/10.1007/BF01886860