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 mMTris-HCl cannot liberate any other proteins than nonadsorbed serum albumin. In conclusion, this investigation demonstrates that immobilized metal ion affinity chromatography with Cu2+, Ni2+, and Fe2+ 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. (C) 2009 Wiley Periodicals, Inc. J Appl Polym Sci 115: 324-329, 2010