Publication:
Investigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates

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dc.contributor.authorOGAN, AYŞE
dc.contributor.authorDANIŞ, ÖZKAN
dc.contributor.authorsAygul I., Karahalil F.Y., Danis O., Ogan A., Kolayli S.
dc.date.accessioned2022-03-15T02:13:48Z
dc.date.accessioned2026-01-11T18:43:01Z
dc.date.available2022-03-15T02:13:48Z
dc.date.issued2018
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.
dc.identifier.doi10.2174/1573408014666180903143132
dc.identifier.issn15734080
dc.identifier.urihttps://hdl.handle.net/11424/247962
dc.language.isoeng
dc.publisherBentham Science Publishers B.V.
dc.relation.ispartofCurrent Enzyme Inhibition
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCarbonic anhydrase
dc.subjectCoumarin
dc.subjectInhibition
dc.subjectJack bean
dc.subjectSynthesis compounds
dc.subjectUrease
dc.titleInvestigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates
dc.typearticle
dspace.entity.typePublication
oaire.citation.endPage232
oaire.citation.issue3
oaire.citation.startPage226
oaire.citation.titleCurrent Enzyme Inhibition
oaire.citation.volume14

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