CHROMATOGRAPHIC PURIFICATION OF IMMUNOGLOBULIN-G FROM BOVINE-MILK WHEY

We used thiophilic chromatography on T-gel, a resin of the structure a garose-O-CH2CH2SO2CH2 CH2SCH2CH2OH, to purify immunoglobulin G from '' sweet'' cheese whey. The purity of immunoglobulin G, as indicated by r adial immunodiffusion, was 74% after a single chromatography on T-gel. Preparation of samples for adsorption onto thiophilic gels requires o nly the addition of salt (sodium/potassium sulfate) to the samples. Th us, this method may be suitable for large-scale whey IgG isolation.