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dc.contributor.authorXie, Jin-Jin
dc.contributor.authorChen, Qing-Xi
dc.contributor.author陈清西
dc.contributor.authorZhang, Ji-Ping
dc.contributor.authorWang, Qin
dc.contributor.author王勤
dc.contributor.authorYang, Xue-Min
dc.date.accessioned2011-08-27T08:44:32Z
dc.date.available2011-08-27T08:44:32Z
dc.date.issued2006
dc.identifier.citationInt J Biol Macromol. 2006 Nov 15;39(4-5):159-64. Epub 2006 Jul 3.zh_CN
dc.identifier.issn0141-8130
dc.identifier.urihttp://dx.doi.org/doi:10.1016/j.ijbiomac.2005.10.006
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10699
dc.description.abstractChemical modification of p-chloromercuribenzoate (PCMB) on beta-N-acetyl-D-glucosaminidase (NAGase, EC 3.2.1.52) from green crab (Scylla serrata) has been studied. The results show that sulfhydryl group is essential for the activity of the enzyme. Inhibitory kinetics of the enzyme by mercuric chloride (HgCl2) has been studied using the kinetic method of the substrate reaction during inhibitor of enzyme. The kinetic results show that the inhibition of the enzyme by mercuric ion (Hg2+) at lower than 1.0 mu M is a reversible reaction with residual activity and the inhibition belongs to be competitive. The inhibition kinetics model of Hg2+ on the enzyme was set up and the microscopic rate constants were determined and the data obtained were well fitted with the model. It was also turned out that only one molecule of HgCl2 binds to the enzyme molecule to lead the enzyme lose its activity. The above results suggest that the cysteine residue is essential for activity and is situated at the active site of the enzyme. (c) 2005 Elsevier B.V. All rights reserved.zh_CN
dc.language.isoenzh_CN
dc.publisherELSEVIER SCIENCE BVzh_CN
dc.subjectgreen crabzh_CN
dc.subjectbeta-N-acetyl-D-glucosaminidasezh_CN
dc.subjectinhibitionzh_CN
dc.subjectkineticszh_CN
dc.subjectmercuric ionzh_CN
dc.titleInhibitory kinetics of mercuric ion on the activity of beta-N-acetyl-D-glucosaminidase from green crab (Scylla serrata)zh_CN
dc.typeArticlezh_CN


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