Chromatographic behavior of mouse serum immunoglobulin G in protein G perfusion affinity chromatography.

In this study chromatographic behavior of mouse serum immunoglobulin G (IgG) on a protein G perfusion affinity chromatographic column was investigated experimentally. The results indicate that the protein G column has no non-specific binding to the other proteins in mouse serum but an irreversible adsorption to IgG under the conditions investigated. It was found that variations of the elution solution composition, ionic strength and pH played to some extent an essential effect on the chromatographic behavior of IgG. The influence of the mobile phase flow-rate on the chromatographic behavior of IgG was also researched. These results show that the dissociation of IgG from protein G affinity packings becomes the rate-limiting step in the perfusion affinity chromatographic separation process.