Show simple item record

dc.contributor.authorZhu, C. M.zh_CN
dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorLin, H. N.zh_CN
dc.contributor.authorYang, Y.zh_CN
dc.contributor.authorPark, Y. D.zh_CN
dc.contributor.authorZhang, R. Q.zh_CN
dc.contributor.authorZhou, H. M.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:35Z
dc.date.available2013-12-12T02:24:35Z
dc.date.issued1999-07zh_CN
dc.identifier.citationJournal of Protein Chemistry, 1999,18(5):603-607zh_CN
dc.identifier.issn0277-8033zh_CN
dc.identifier.otherISI:000083114100011zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65664
dc.description.abstractThe inhibition of alkaline phosphatase from green crab (Scylla serrata) by L-cysteine has been studied. The results show that L-cysteine gives a mixed-type inhibition. The progress-of-substrate-reaction method previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mel. Biol. 61, 391-436] was used to study the inactivation kinetics of the enzyme by L-cysteine. The microscopic rate constants were determined for reaction of the inhibitor with the free enzyme and the enzyme-substrate complex (ES) The results show that inactivation of the enzyme by L-cysteine is a slow., reversible reaction. Comparison of the inactivation rate constants of free enzyme and ES suggests that the presence of the substrate offers marked protection of this enzyme against inactivation by L-cysteine.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1023/A:1020611602818zh_CN
dc.subjectIONSzh_CN
dc.titleKinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by L-cysteinezh_CN
dc.typeArticlezh_CN


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record