DSpace at EWHA: Determination of the pKa for histidine-51 residue in the ternary complex of horse liver alcohol dehydrogenase

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DC Field	Value	Language
dc.contributor.author	이강만	-
dc.date.accessioned	2018-06-02T08:15:29Z	-
dc.date.available	2018-06-02T08:15:29Z	-
dc.date.issued	1992	-
dc.identifier.issn	0253-6269	-
dc.identifier.other	OAK-16847	-
dc.identifier.uri	https://dspace.ewha.ac.kr/handle/2015.oak/244536	-
dc.description.abstract	The pKa value of histidine-51 residue was determined by the pH dependency of contents of NADH bound to the active site in the horse liver alcohol dehydrogenase and % inactivation with diethyl pyrocarbonate treatment of the enzyme. The pKa for His-51 was ~7.15 in the ternary complex and ~6.7 in the enzyme itself.	-
dc.language	English	-
dc.title	Determination of the pKa for histidine-51 residue in the ternary complex of horse liver alcohol dehydrogenase	-
dc.type	Article	-
dc.relation.issue	3	-
dc.relation.volume	15	-
dc.relation.index	SCIE	-
dc.relation.index	SCOPUS	-
dc.relation.index	KCI	-
dc.relation.startpage	229	-
dc.relation.lastpage	233	-
dc.relation.journaltitle	Archives of Pharmacal Research	-
dc.identifier.scopusid	2-s2.0-0026984463	-
dc.author.google	Lee K.M.	-
dc.author.google	Son S.Y.	-
dc.contributor.scopusid	이강만(7501506362)	-
dc.date.modifydate	20180601095152	-