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dc.contributor.authorXie, XL
dc.contributor.authorGong, M
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.date.accessioned2011-09-16T08:03:58Z
dc.date.available2011-09-16T08:03:58Z
dc.date.issued2006
dc.identifier.citationJournal of Enzyme Inhibition and Medicinal Chemistry (2006)Volume: 21, Issue: 1, Pages: 55-60zh_CN
dc.identifier.issn1475-6366
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10748
dc.description.abstractThe effects of hydrogen peroxide (H2O2) on prawn NAGase activity for the hydrolysis of pNP-beta-D-GlcNAc have been studied. The results show that H2O2 can reversible inhibit the enzyme (IC50 similar or equal to 0.85 M) and the inhibition is of a mixed type. The kinetics show that k(+0) is much larger than k'(+0), indicating the free enzyme is more susceptible than the enzyme-substrate complex in the H2O2 solution. It is suggested that the presence of the substrate offers marked protection against inhibition by H2O2. Changes of activity and conformation of the enzyme in different concentrations of H2O2 have been compared by measuring the fluorescence spectra and residual activity and show that the change of conformation is more rapidly than that of the residual activity, which implies that the whole conformation of the enzyme changes more rapidly than the conformation of the active centre of the enzyme in the H2O2 solution.zh_CN
dc.language.isoenzh_CN
dc.publisherTAYLOR & FRANCIS LTDzh_CN
dc.subjectPenaeus vannameizh_CN
dc.subjectbeta-N-acetyl-D-glucosaminidasezh_CN
dc.subjectinhibition kineticszh_CN
dc.subjecthydrogen peroxidezh_CN
dc.subjectconformationzh_CN
dc.subjectactivityzh_CN
dc.titleInhibition kinetics of hydrogen peroxide on beta-N-acetyl-D-glucosaminidase from prawn (Penaeus vannamei)zh_CN
dc.typeArticlezh_CN


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