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dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorHuang, H.zh_CN
dc.contributor.authorKubo, I.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.issued2003-07zh_CN
dc.identifier.citationJournal of Protein Chemistry, 2003,22(5):481-487zh_CN
dc.identifier.issn0277-8033zh_CN
dc.identifier.otherISI:000186865700011zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65660
dc.description.abstractCetylpyridinium chloride (CPC) was found to inactivate tyrosinase from mushroom ( Agaricus bisporus). CPC can bind to the enzyme molecule and induce the enzyme conformation changes. The fluorescence intensity ( at 338.4 nm) of the enzyme decreased distinctly with increasing CPC concentrations, and a new little fluorescence emission peak appeared near 372 nm. The inactivation of the enzyme by CPC had first been studied by using the kinetic method of the substrate reaction described by Tsou. The results showed that the enzyme was inactivated by a complex mechanism that had not been previously identified. The enzyme first quickly binds with CPC reversibly and then undergoes a slow irreversible inactivation. The inactivation reaction is a single molecule reaction and the apparent inactivation rate constant is a saturated trend being independent of CPC concentration if the concentration is sufficiently high. The micro rate constants of inactivation and the association constant were determined.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1023/B:JOPC.0000005464.36961.9czh_CN
dc.subjectSERRATA ALKALINE-PHOSPHATASEzh_CN
dc.subjectSODIUM DODECYL-SULFATEzh_CN
dc.subjectAGARICUS-BISPORUSzh_CN
dc.subjectPOLYPHENOL OXIDASEzh_CN
dc.subjectINHIBITIONzh_CN
dc.subjectACTIVATIONzh_CN
dc.subjectCRABzh_CN
dc.subjectPROPHENOLOXIDASEzh_CN
dc.subjectSUBSTRATEzh_CN
dc.subjectHEMOLYMPHzh_CN
dc.titleInactivation kinetics of mushroom tyrosinase by cetylpyridinium chloridezh_CN
dc.typeArticlezh_CN


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