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dc.contributor.authorÖzensoy, Özen
dc.contributor.authorArslan, Oktay
dc.contributor.authorIşık, Semra
dc.contributor.authorArslan, Mikail
dc.contributor.authorScozzafava, Andrea
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2019-10-17T08:04:34Z
dc.date.available2019-10-17T08:04:34Z
dc.date.issued2005en_US
dc.identifier.issn1475-6366
dc.identifier.issn1475-6374
dc.identifier.urihttps://doi.org/ 10.1080/14756360500141960
dc.identifier.urihttps://hdl.handle.net/20.500.12462/7851
dc.descriptionÖzensoy, Özen (Balıkesir Author)en_US
dc.description.abstractThe purification of red blood cell carbonic anhydrase (CA, EC 4.2. 1. 1) from ostrich (scCA) blood is reported, as well as an inhibition study of this enzyme with a series of aromatic and heterocylic sulfonamides. The ostrich enzyme showed a high activity, comparable to that of the human isozyme II, with k(cat) of 1. 2 center dot 10(6) s(-1) and k(cat)/K-M of 1. 8 center dot 10(7)M(-1) s(-1), and an inhibition profile quite different from that of the human red blood cell cytosolic isozymes hCA I and II. scCA has generally a lower affinity for sulfonamide inhibitors as compared to hCA I and II. The only sulfonamide which behaved as a very potent inhibitor of this enzyme was ethoxzolamide (K-1 = 3.9 nM) whereas acetazolamide and sulfanilamide behaved as weaker inhibitors (inhibition constants in the range 303-570 nM). Several other aromatic and heterocyclic sulfonamides, mostly derivatives of sulfanilamide, homosulfanilamide, 4-aminoethylbenzenesulfonamide or 5-amino-1,3,4-thiadiazole-2-sulfonamide, showed good affinities for the ostrich enzyme, with K-1 values in the range 25 - 72 nM.en_US
dc.language.isoengen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.isversionof10.1080/14756360500141960en_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCarbonic Anhydraseen_US
dc.subjectSulfonamideen_US
dc.subjectOstrichen_US
dc.subjectInhibitoren_US
dc.subjectEnzyme İnhibitionen_US
dc.titleCarbonic anhydrase inhibitors. Inhibition of red blood cell ostrich (Struthio camelus) carbonic anhydrase with a series of aromatic and heterocyclic sulfonamidesen_US
dc.typearticleen_US
dc.relation.journalJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.contributor.departmentFen Edebiyat Fakültesien_US
dc.contributor.authorID0000-0001-5020-3322en_US
dc.identifier.volume20en_US
dc.identifier.issue4en_US
dc.identifier.startpage383en_US
dc.identifier.endpage387en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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