dc.contributor.author | Şahin, Ayşegül | |
dc.contributor.author | Işık, Semra | |
dc.contributor.author | Arslan, Oktay | |
dc.contributor.author | Supuran, Claudiu T. | |
dc.contributor.author | Güler, Özen Özensoy | |
dc.date.accessioned | 2019-10-17T10:37:18Z | |
dc.date.available | 2019-10-17T10:37:18Z | |
dc.date.issued | 2015 | en_US |
dc.identifier.issn | 1475-6366 | |
dc.identifier.issn | 1475-6374 | |
dc.identifier.uri | https://doi.org/10.3109/14756366.2014.912215 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12462/8187 | |
dc.description.abstract | The new affinity gel reported in this study was prepared using EUPERGIT C250L as a chromatographic bed material, to which etylenediamine spacer arms were attached to prevent steric hindrance between the matrix and ligand, and to facilitate effective binding of the CA-specific ligand, of the aromatic sulfonamide type for the purification of alpha-carbonic anhydrases (Cas; EC 4.2.1.1). Indeed, the aminoethyl moieties of the affinity gel were derivatized by reaction with 4-isothiocyanatobenzenesulfonamide, with the formation of a thiourea-based gel, having inhibitory effects against CAs. Both bovine erythrocyte carbonic anhydrase BCA and human (h) erythrocyte CA isoforms I, II (hCA I and II) have been purified from hemolysates, by using this affinity gel. The greatest purification fold and column yields for BCA and for cytosolic (hCA I + II) enzymes were of 181-fold (21.07%) and 184-fold (9.49%), respectively. Maximum binding was achieved at 15 degrees C and I = 0.3 ionic strength for alpha-carbonic anhydrases. | en_US |
dc.description.sponsorship | Şahin, Ayşegül (Balikesir Author) | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Taylor & Francis Ltd | en_US |
dc.relation.isversionof | 10.3109/14756366.2014.912215 | en_US |
dc.rights | info:eu-repo/semantics/embargoedAccess | en_US |
dc.subject | Affinity Chromatography | en_US |
dc.subject | Carbonic Anhydrase | en_US |
dc.subject | Purification | en_US |
dc.title | A new affinity gel for the purification of alpha-carbonic anhdrases | en_US |
dc.type | article | en_US |
dc.relation.journal | Journal of Enzyme Inhibition and Medicinal Chemistry | en_US |
dc.contributor.department | Fen Edebiyat Fakültesi | en_US |
dc.identifier.volume | 30 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.startpage | 224 | en_US |
dc.identifier.endpage | 228 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |