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
✍ Scribed by Noureddine Charef; Lekhmici Arrar; Afaf Lamaaoui; Hiba Boudjellal; Abderrahmane Baghiani; Nadjet Hanachi; Sabah Boumerfeg; Seddik Khennouf; Mohammad S. Mubarak
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 199 KB
- Volume
- 115
- Category
- Article
- ISSN
- 0021-8995
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✦ Synopsis
Abstract
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