Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide |
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Authors: | Qing-Xi Chen Wei Zhang Wen-Zhu Zheng Hong Zhao Si-Xu Yan Hong-Rui Wang Hai-Meng Zhou |
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Institution: | 1. Department of Biology, Xiamen University, 361005, Xiamen, China 2. Department of Biological Science and Biotechnology, Tsinghua University, 100084, Beijing, China
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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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