Inhibition studies on mutant Phe91Asn human carbonic anhydrase I (HCA I) gene

dc.contributor.authorKöçkar, Feray
dc.contributor.authorAyduen, M.
dc.contributor.authorTürkoğlu, Sümeyye Aydoğan
dc.contributor.authorArslan, Oktay
dc.contributor.authorTuran, Yusuf
dc.date.accessioned2019-10-17T11:10:05Z
dc.date.available2019-10-17T11:10:05Z
dc.date.issued2008en_US
dc.departmentFakülteler, Fen-Edebiyat Fakültesi, Kimya Bölümüen_US
dc.departmentFakülteler, Fen-Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractCarbonic anhydrases (CAs; carbonate dehydratases EC 4.2.1.1) are ubiquitous metalloenzymes present in prokaryotes and eukaryotes that and encoded by four evolutionarily different gene families. In mammals, 15 a-CA isozymes or CA-related proteins have been described, with different catalytic activity, subcellular localization and tissue distribution. CAI is a member of a-CA family and situated on the long arm of chromosome 8. It presents in erythrocytes, colon epithelium, lens of eye and corneal epithelium and the most abundant protein after hemoglobin in erythrocytes.en_US
dc.identifier.endpage168en_US
dc.identifier.issn1742-464X
dc.identifier.issue1en_US
dc.identifier.startpage168en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12462/8483
dc.identifier.volume275en_US
dc.identifier.wosWOS:000256633300517
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.language.isoenen_US
dc.publisherWiley-Blackwellen_US
dc.relation.ispartofFebs Journalen_US
dc.relation.publicationcategoryDiğeren_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBiochemistry & Molecular Biologyen_US
dc.titleInhibition studies on mutant Phe91Asn human carbonic anhydrase I (HCA I) geneen_US
dc.typeOtheren_US

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