Chromatographic purification of immunoglobulin G from bovine milk whey

Abstract

We used thiophilic chromatography on T-gel, a resin of the structure agarose-O-CH2CH2SO2CH2 CH2SCH2CH2OH, to purify immunoglobulin G from "sweet" cheese whey. The purity of immunoglobulin G, as indicated by radial immunodiffusion, was 74% after a single chromatography on T-gel. Preparation of samples for adsorption onto thiophilic gels requires only the addition of salt (sodium/potassium sulfate) to the samples. Thus, this method may be suitable for large-scale whey IgG isolation. © 1994.