| dc.contributor.author | Köçkar, Feray | |
| dc.contributor.author | Ayduen, M. | |
| dc.contributor.author | Türkoğlu, Sümeyye Aydoğan | |
| dc.contributor.author | Arslan, Oktay | |
| dc.contributor.author | Turan, Yusuf | |
| dc.date.accessioned | 2019-10-17T11:10:05Z | |
| dc.date.available | 2019-10-17T11:10:05Z | |
| dc.date.issued | 2008 | en_US |
| dc.identifier.issn | 1742-464X | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12462/8483 | |
| dc.description.abstract | Carbonic 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.language.iso | eng | en_US |
| dc.publisher | Wiley-Blackwell | en_US |
| dc.rights | info:eu-repo/semantics/openAccess | en_US |
| dc.subject | Biochemistry & Molecular Biology | en_US |
| dc.title | Inhibition studies on mutant Phe91Asn human carbonic anhydrase I (HCA I) gene | en_US |
| dc.type | other | en_US |
| dc.relation.journal | Febs Journal | en_US |
| dc.contributor.department | Fen Edebiyat Fakültesi | en_US |
| dc.identifier.volume | 275 | en_US |
| dc.identifier.issue | 1 | en_US |
| dc.identifier.startpage | 168 | en_US |
| dc.identifier.endpage | 168 | en_US |
| dc.relation.publicationcategory | Diğer | en_US |
