Comparison of hydratase, esterase activities and inhibition manner of mutant Asn67/Ile and Leu204/Ser of human CAII

dc.contributor.authorTürkoğlu, Sumeyye Aydoğan
dc.contributor.authorKöçkar, Feray
dc.contributor.authorAydın, Meltem
dc.contributor.authorSinan, Selma
dc.contributor.authorArslan, Oktay
dc.date.accessioned2019-10-17T11:10:13Z
dc.date.available2019-10-17T11:10:13Z
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; also known as carbonate dehydratases EC 4.2.1.1) are a family of enzymes which catalyze the reversible reaction from H2O and CO2 to HCO3 - ions. Carbonic anhydrases are ubiquitous metalloenzymes present in prokaryotes and eukaryotes that are encoded by five evolutionarily unrelated gene families, namely a- CAs, b-CAs, c-CAs, d-CAs and e-CAs. In mammals, 15 a-CA isozymes or CA-related proteins have been described with different catalytic activity, subcellular localization and tissue distribution.en_US
dc.identifier.endpage157en_US
dc.identifier.issn1742-464X
dc.identifier.issue1en_US
dc.identifier.startpage157en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12462/8487
dc.identifier.volume275en_US
dc.identifier.wosWOS:000256633300475
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.language.isoenen_US
dc.publisherBlackwell Publishingen_US
dc.relation.ispartofFebs Journalen_US
dc.relation.publicationcategoryDiğeren_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBiochemistry & Molecular Biologyen_US
dc.titleComparison of hydratase, esterase activities and inhibition manner of mutant Asn67/Ile and Leu204/Ser of human CAIIen_US
dc.typeOtheren_US

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