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dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorZhang, W.zh_CN
dc.contributor.authorWang, H. R.zh_CN
dc.contributor.authorZhou, H. M.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:33Z
dc.date.available2013-12-12T02:24:33Z
dc.date.issued1996-12zh_CN
dc.identifier.citationInternational Journal of Biological Macromolecules, 1996,19(4):257-261zh_CN
dc.identifier.issn0141-8130zh_CN
dc.identifier.otherISI:A1996WE38400005zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65629
dc.description.abstractGreen crab (Scylla Serrata) alkaline phosphatase (EC 3.1.3.1.) is a metalloenzyme, the each active site in which contains a tight cluster of two zinc ions and one magnesium ion. The kinetic theory of the substrate reaction during irreversible inhibition of enzyme activity previously described by Tsou has been applied to a study on the kinetics of the course of inactivation of the enzyme by ethylenediaminetetraacetic acid disodium (EDTA). The kinetics of the substrate reaction with different concentrations of the substrate p-nitrophenyl phosphate (PNPP) and inactivator EDTA suggested a complexing mechanism for inactivation by, and substrate competition with, EDTA at the active site. The inactivation kinetics are single phasic, showing the initial formation of an enzyme-EDTA complex is a relatively rapid reaction, followed a slow inactivation step that probably involves a conformational change of the enzyme. Zinc ions are finally removed from the enzyme. The presence of metal ions apparently stabilizes an active-site conformation required for enzyme activity. Copyright (C) 1996 Elsevier Science B.V.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1016/S0141-8130(96)01135-Xzh_CN
dc.subjectAMINOACYLASEzh_CN
dc.subject1,10-PHENANTHROLINEzh_CN
dc.titleKinetics of inactivation of green crab (Scylla Serrata) alkaline phosphatase during removal of zinc ions by ethylenediaminetetraacetic acid disodiumzh_CN
dc.typeArticlezh_CN


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