Abstract
The amino acid ortho-phosphoserine (OPS) is a feasible alternative to expensive protein ligands for the purification of IgG due to its selectivity, elution under non-denaturing conditions, and low cost. In this study we investigated the adsorption of IgG2a mouse monoclonal antibody (MAb) from precipitate solution of hybridoma culture supernatant onto OPS-agarose adsorbent. The effects of spacer arm, buffer system, pH, and NaCl concentration on the adsorption of IgG2a MAb were evaluated. Screening buffer systems showed that Tris–HCl at pH 7.0 provided the highest IgG2a MAb yield (77%) and purification factor (31.8). The adsorption of IgG2a MAb was observed to decrease by approximately 90% as the NaCl concentration was increased from 0.0 to 100mmolL−1. A kinetic study of IgG2a MAb adsorption showed that these data were in agreement with the pseudo-first-order kinetic model. This study suggests the potential for use of OPS-agarose in the purification of IgG2a MAb from hybridoma culture supernatants.
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