Inactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site.

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dc.contributor.authorKumble, K Den_US
dc.contributor.authorKumble, Sen_US
dc.contributor.authorJaffar, M Ben_US
dc.date.accessioned2009-05-28T13:05:58Z
dc.date.available2009-05-28T13:05:58Z
dc.date.issued1992-02-01en_US
dc.description.abstractModification of A. conoides beta-glucosidase by diethylpyrocarbonate caused rapid inactivation of the enzyme. The kinetic analyses showed that the inactivation by diethylpyrocarbonate resulted from the modification of an average of one histidine residue per mole of enzyme. The modified enzyme showed an increase in absorbance at 240 nm. Sulphydryl, lysine and tyrosine residues were not modified by diethylpyrocarbonate treatment. The substrate offered significant protection against diethylpyrocarbonates modification. The results indicate that diethylpyrocarbonate was interacting with the enzyme at or near the active site.en_US
dc.description.affiliationDepartment of Biochemistry, Wilson College, Bombay, India.en_US
dc.identifier.citationKumble KD, Kumble S, Jaffar MB. Inactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site. Indian Journal of Experimental Biology. 1992 Feb; 30(2): 99-102en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/58961
dc.language.isoengen_US
dc.source.urihttps://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijeb/ijeb0.aspen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshDiethyl Pyrocarbonate --pharmacologyen_US
dc.subject.meshHistidine --physiologyen_US
dc.subject.meshIodoacetamide --pharmacologyen_US
dc.subject.meshMitosporic Fungi --enzymologyen_US
dc.subject.meshNitrophenylgalactosides --pharmacologyen_US
dc.subject.meshPyridoxal Phosphate --pharmacologyen_US
dc.subject.meshbeta-Glucosidase --drug effectsen_US
dc.titleInactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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