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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
Author(s) -
Charef Noureddine,
Arrar Lekhmici,
Lamaaoui Afaf,
Boudjellal Hiba,
Baghiani Abderrahmane,
Hanachi Nadjet,
Boumerfeg Sabah,
Khennouf Seddik,
Mubarak Mohammad S.
Publication year - 2009
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.31124
Subject(s) - amberlite , chemistry , chromatography , adsorption , elution , metal ions in aqueous solution , bovine serum albumin , human serum albumin , ion exchange resin , ion exchange , ion chromatography , tris , column chromatography , metal , ion , inorganic chemistry , organic chemistry , biochemistry
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