Effect of adsorbed metal ions and buffer nature on IgG separation from human plasma by column chromatography using an ion exchange resin, Amberlite IRC‐718

Fractionation of human plasma on ion exchanger resin was performed on Amberlite IRC‐718 saturated with metal ions. Depletion of human immunoglobulin G was carried out by column chromatography using Tris‐HCl, pH 7 at different concentrations. Results showed that, when Cu +2 and Ni +2 were adsorbed on the resin, one or two fractions of purified IgG were obtained, respectively. Whereas Fe +2 and Zn +2 , both retain IgG and serum albumin or serum albumin alone. Furthermore, the Ni +2 ‐resin retention of serum proteins is too strong that the use of 700 m M Tris‐HCl cannot liberate any other proteins than nonadsorbed serum albumin. In conclusion, this investigation demonstrates that immobilized metal ion affinity chromatography with Cu 2+ , Ni 2+ , and Fe 2+ immobilized on Amberlite IRC‐718 has the potential to be developed as part of a process to purify IgG out of untreated human plasma as acceptable adsorption and elution levels of IgG could be achieved. © 2009 Wiley Periodicals, Inc. J Appl Polym Sci, 2010