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 þ2 and Ni þ2 were adsorbed on the resin, one or two fractions of purified IgG were obtained, respectively. Whereas Fe þ2 and Zn þ2 , both retain IgG and serum albumin or serum albumin alone. Furthermore, the Ni þ2 -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 Cu 2þ , Ni 2þ , and Fe 2þ 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.
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