| dc.contributor.author | Türkoğlu, Sumeyye Aydoğan | |
| dc.contributor.author | Köçkar, Feray | |
| dc.contributor.author | Aydın, Meltem | |
| dc.contributor.author | Sinan, Selma | |
| dc.contributor.author | Arslan, Oktay | |
| dc.date.accessioned | 2019-10-17T11:10:13Z | |
| dc.date.available | 2019-10-17T11:10:13Z | |
| dc.date.issued | 2008 | en_US |
| dc.identifier.issn | 1742-464X | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12462/8487 | |
| dc.description.abstract | Carbonic 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.language.iso | eng | en_US |
| dc.publisher | Blackwell Publishing | en_US |
| dc.rights | info:eu-repo/semantics/openAccess | en_US |
| dc.subject | Biochemistry & Molecular Biology | en_US |
| dc.title | Comparison of hydratase, esterase activities and inhibition manner of mutant Asn67/Ile and Leu204/Ser of human CAII | 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 | 157 | en_US |
| dc.identifier.endpage | 157 | en_US |
| dc.relation.publicationcategory | Diğer | en_US |
