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dc.contributor.authorChen, Q. X.zh_CN
dc.contributor.authorZhang, Z.zh_CN
dc.contributor.authorZhou, X. W.zh_CN
dc.contributor.authorZhuang, Z. L.zh_CN
dc.contributor.author陈清西zh_CN
dc.date.accessioned2013-12-12T02:24:33Z
dc.date.available2013-12-12T02:24:33Z
dc.date.issued2000-07zh_CN
dc.identifier.citationInternational Journal of Biochemistry & Cell Biology, 2000,32(7):717-723zh_CN
dc.identifier.issn1357-2725zh_CN
dc.identifier.otherISI:000087825800004zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65630
dc.description.abstractThe kinetics of inhibition of beta-glucosidase from Ampullarium crossean by bromoacetic acid (BrAc) has been studied. The results show that the enzyme can be irreversibly and completely inactivated at high BrAc concentration, while at low BrAc concentration, inhibition of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reactions of BrAc with the enzyme were determined. The presence of the substrate offers obvious protection of the enzyme against inhibition by BrAc. The above results suggest that the histidine residue is essential for activity and is situated at or near the active site of the enzyme. (C) 2000 Elsevier Science Ltd. All rights reserved.zh_CN
dc.language.isoen_USzh_CN
dc.source.urihttp://dx.doi.org/10.1016/S1357-2725(00)00020-0zh_CN
dc.subjectCRAB SCYLLA-SERRATAzh_CN
dc.subjectALKALINE-PHOSPHATASEzh_CN
dc.subjectTRICHODERMA-REESEIzh_CN
dc.subjectCELLULASESzh_CN
dc.titleKinetics of inhibition of beta-glucosidase from Ampullarium crossean by bromoacetic acidzh_CN
dc.typeArticlezh_CN


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