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dc.creatorMomić, Tatjana
dc.creatorVujčić, Zoran
dc.creatorVasić, Vesna M.
dc.date.accessioned2018-03-01T20:27:05Z
dc.date.available2018-03-01T20:27:05Z
dc.date.issued2008
dc.identifier.issn0538-8066 (print)
dc.identifier.urihttp://vinar.vin.bg.ac.rs/handle/123456789/3464
dc.description.abstractThe inhibition of myeloperoxidase (MPO), isolated from human neutrophils, by quercetin was investigated by following peroxidase activity of the enzyme using o-dianisidine as the substrate. The inhibition parameters (IC(50)) were obtained by graphical analysis of the inhibition curves. A reaction mechanism, which involved the enzyme inhibition by quercetin and H(2)O(2) in excess, was proposed. The rate and equilibrium constants for the proposed reaction path were calculated from experimental data. Kinetic analysis in noninhibiting H(2)O(2) concentration range in the absence and the presence of quercetin revealed that the reaction mechanism underwent Michaelis-Menten kinetics. K(m)(app,H2O2) and V(max)(app) values indicated that quercetin was a mixed inhibitor of MPO activity. The initial reaction rates were recalculated using the obtained results. Calculated curves fitted the experimental results within the range of experimental error. (C) 2008 Wiley Periodicals, Inc.en
dc.rightsrestrictedAccessen
dc.sourceInternational Journal of Chemical Kineticsen
dc.titleKinetics of inhibition of peroxidase activity of myeloperoxidase by quercetinen
dc.typearticleen
dcterms.abstractМомић Татјана; Вујциц, Зоран; Васић Весна М;
dc.citation.volume40
dc.citation.issue7
dc.citation.spage384
dc.citation.epage394
dc.identifier.wos000256689400003
dc.identifier.doi10.1002/kin.20319
dc.citation.rankM23
dc.identifier.scopus2-s2.0-45749100912


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