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dc.contributor.authorChen, S. L.zh_CN
dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorYang, P. Z.zh_CN
dc.contributor.authorQiu, W. J.zh_CN
dc.contributor.authorWang, L. T.zh_CN
dc.contributor.authorZhou, H. M.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:34Z
dc.date.available2013-12-12T02:24:34Z
dc.date.issued1997-07zh_CN
dc.identifier.citationBiochemistry and Molecular Biology International, 1997,42(3):517-526zh_CN
dc.identifier.issn1039-9712zh_CN
dc.identifier.otherISI:000072915100009zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65647
dc.description.abstractThe conformational changes of penaeus penicillatus acid phosphatase during denaturation in guanidine hydrochloride solutions were studied by following changes in the intrinsic fluorescence, ultraviolet difference absorption, and circular dichroism spectra. Inactivation of the enzyme in guanidine hydrochloride solutions were compared with unfolding of the enzyme molecule. The results show that the extent of unfolding in guanidine solutions measured by several different methods closely coincide with each other and that slightly lower concentrations of guanidine are required to bring about inactivation than are required to produce significant conformational changes of the enzyme molecule. At the same concentrations, the inactivation rate constants are markedly faster than the rate constants for unfolding of the enzyme. The above results suggest that the active sites of this enzyme display more conformational flexxibility than the enzyme molecule as a whole.zh_CN
dc.language.isoen_USzh_CN
dc.subjectCONFORMATIONAL CHANGEzh_CN
dc.subjectCREATINE-KINASEzh_CN
dc.subjectACTIVE-SITESzh_CN
dc.subjectCHLORIDEzh_CN
dc.subjectRATESzh_CN
dc.subjectAMINOACYLASEzh_CN
dc.titleUnfolding and inactivation of penaeus penicillatus acid phosphatase during denaturation by guanidine hydrochloridezh_CN
dc.typeArticlezh_CN


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