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dc.contributor.authorTaslimi, Parham
dc.contributor.authorGulcin, Ilhami
dc.contributor.authorOztaskin, Necla
dc.contributor.authorCetinkaya, Yasin
dc.contributor.authorGoksu, Suleyman
dc.contributor.authorAlwasel, Saleh H.
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2019-06-13T06:31:17Z
dc.date.available2019-06-13T06:31:17Z
dc.date.issued2016
dc.identifier.urihttp://hdl.handle.net/11772/1385
dc.description.abstractCarbonic anhydrases (CAs, EC 4.2.1.1), which are involved in a variety of physiological and pathological processes, are ubiquitous metalloenzymes mainly catalyzing the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3-) and proton (H+). In this study, a dozen of bromophenol derivatives (1-12) were evaluated as metalloenzyme CA (EC 4.2.1.1) inhibitors against the human carbonic anhydrase isoenzymes I and II (hCA I and II). Cytosolic hCA I and II isoenzymes were effectively inhibited by bromophenol derivatives (1-12) with K-is in the low nanomolar range of 1.85 +/- 0.58 to 5.04 +/- 1.46 nM against hCA I and in the range of 2.01 +/- 0.52 to 2.94 +/- 1.31 nM against hCA II, respectively.en_US
dc.language.isoengen_US
dc.publisherInformaen_US
dc.relation.isversionof10.3109/14756366.2015.1054820en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectBromophenolsen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectEnzyme inhibitionen_US
dc.subjectEnzyme purificationen_US
dc.subjectIsoenzymesen_US
dc.titleThe effects of some bromophenols on human carbonic anhydrase isoenzymesen_US
dc.typearticleen_US
dc.relation.journalJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.contributor.departmentBartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümüen_US
dc.identifier.volume31en_US
dc.identifier.issue4en_US
dc.identifier.startpage603en_US
dc.identifier.endpage607en_US


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