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dc.creatorPavelkic, V. M.
dc.creatorKrinulovic, K. S.
dc.creatorSavić, Jasmina
dc.creatorIlic, M. A.
dc.date.accessioned2018-03-01T20:25:22Z
dc.date.available2018-03-01T20:25:22Z
dc.date.issued2008
dc.identifier.issn0036-0244 (print)
dc.identifier.urihttp://vinar.vin.bg.ac.rs/handle/123456789/3444
dc.description.abstractThe in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC (50) values as calculated from the experimental inhibition curves were 1.33 x 10(-9) and 1.48 x 10(-5) M for the high-and low-affinity binding sites, respectively; Hills analysis gave 1.29 x 10(-9) and 1.38 x 10(-6) M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites.en
dc.rightsrestrictedAccessen
dc.sourceRussian Journal of Physical Chemistry Aen
dc.titleMalathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy methoden
dc.typearticleen
dcterms.abstractПавелкиц, В. М.; Кринуловиц, К. С.; Илиц, М. A.; Савић Јасмина;
dc.citation.volume82
dc.citation.issue5
dc.citation.spage870
dc.citation.epage874
dc.identifier.wos000255747800031
dc.identifier.doi10.1134/S0036024408050312
dc.citation.rankM23
dc.identifier.scopus2-s2.0-43449130920


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