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dc.contributor.authorZhou, X. W.zh_CN
dc.contributor.authorZhuang, Z. L.zh_CN
dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:34Z
dc.date.available2013-12-12T02:24:34Z
dc.date.issued1999-10zh_CN
dc.identifier.citationJournal of Protein Chemistry, 1999,18(7):735-740zh_CN
dc.identifier.issn0277-8033zh_CN
dc.identifier.otherISI:000085128600002zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65659
dc.description.abstractGreen crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspecific hydrolysis of phosphate monoesters. The kinetics of inhibition of the enzyme by sodium (2, 2'-bipyridine) oxodiperoxovanadate, pV(bipy), has been studied. The time course of the hydrolysis of p-nitrophenyl-phosphate catalyzed by the enzyme in the presence of different pV(bipy) concentrations showed that at each pV(bipy) concentration, the rate decreased with increasing time until a straight line was approached, the straight line slopes are the same for all concentrations. The results suggest that the inhibition of the enzyme by pV(bipy) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined for the reaction of inhibitor with the enzyme.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1023/A:1020621332377zh_CN
dc.subjectINACTIVATIONzh_CN
dc.titleKinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by sodium (2,2 '-bipyridine) oxodiperoxovanadatezh_CN
dc.typeArticlezh_CN


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