AI Article Synopsis
- The study introduces a new affinity gel made from EUPERGIT C250L that utilizes etylenediamine arms to enhance binding efficiency of a specific ligand for purifying α-carbonic anhydrases (CAs).
- The gel is modified by incorporating 4-isothiocyanatobenzenesulfonamide, resulting in a thiourea-based structure with inhibitory effects on CAs.
- The affinity gel successfully purified both bovine and human carbonic anhydrase with notable purification folds of 181-fold and 184-fold, respectively, under optimal conditions of 15°C and ionic strength of 0.3.
Article 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 α-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 °C and I = 0.3 ionic strength for α-carbonic anhydrases.
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| http://dx.doi.org/10.3109/14756366.2014.912215 | DOI Listing |
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