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dc.contributor.authorAygul, I.
dc.contributor.authorKarahalil, F.Y.
dc.contributor.authorDanis, O.
dc.contributor.authorOgan, A.
dc.contributor.authorKolayli, S.
dc.date.accessioned2021-11-09T19:37:24Z
dc.date.available2021-11-09T19:37:24Z
dc.date.issued2018
dc.identifier.issn15734080
dc.identifier.urihttps://hdl.handle.net/20.500.12440/2883
dc.description.abstractIntroduction: This study investigated the in vitro inhibition properties of newly synthesized coumarin derivates (C1-C5) against human carbonic anhdyrase I (hCA-I) and jack bean urease. Activities were expressed as IC50 (mg/mL), the concentration reducing 50% of the enzymes. The IC50 values for hCA-I ranged 5.20 µM from 12.10 µM, with compound C3 exhibiting the highest activity. The inhibition values for urease ranged 22.30 µM to 39.00 µM, the highest activity being observed in C5. Conclusion: Comparing the inhibitions with standard inhibitors of the enzymes, while the samples exhibited moderate inhibitions against hCA I, high inhibition was determined against urease. © 2018 Bentham Science Publishers.en_US
dc.language.isoengen_US
dc.publisherBentham Science Publishers B.V.en_US
dc.relation.ispartofCurrent Enzyme Inhibitionen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCarbonic anhydrase; Coumarin; Inhibition; Jack bean; Synthesis compounds; Ureaseen_US
dc.titleInvestigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivatesen_US
dc.typearticleen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.description.scopuspublicationid2-s2.0-85062830056en_US
dc.department[Belirlenecek]en_US
dc.identifier.volume14en_US
dc.identifier.issue3en_US
dc.identifier.startpage226en_US
dc.contributor.institutionauthor[Belirlenecek]
dc.identifier.doi10.2174/1573408014666180903143132
dc.identifier.endpage232en_US
dc.authorscopusid57190816353
dc.authorscopusid54395485300
dc.authorscopusid26638740000
dc.authorscopusid13409447800
dc.authorscopusid6603002455


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