Please use this identifier to cite or link to this item: https://open.uns.ac.rs/handle/123456789/14939
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dc.contributor.authorPantelić, M.en_US
dc.contributor.authorTrivić S.en_US
dc.contributor.authorLeskovac V.en_US
dc.date.accessioned2020-03-03T14:57:57Z-
dc.date.available2020-03-03T14:57:57Z-
dc.date.issued1996-12-01-
dc.identifier.issn03525139en_US
dc.identifier.urihttps://open.uns.ac.rs/handle/123456789/14939-
dc.description.abstractp-Nitrosophenol is easily reduced by NADH in the presence of equine liver alcohol dehydrogenase (EC 1.1.1.1). In this work we report the steady-state kinetic parameters for this enzymatic reaction at pH 7.0, and the pH-profile of its catalytic constant. In addition, the minimal chemical mechanism of this reaction is postulated.en_US
dc.relation.ispartofJournal of the Serbian Chemical Societyen_US
dc.titleReduction of p-nitrosophenol by NADH catalyzed by equine liver alcohol dehydrogenaseen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.scopus2-s2.0-0030506177-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/0030506177-
dc.description.versionUnknownen_US
dc.relation.lastpage863en_US
dc.relation.firstpage859en_US
dc.relation.issue10en_US
dc.relation.volume61en_US
item.grantfulltextnone-
item.fulltextNo Fulltext-
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