Chromatographic purification of immunoglobulin G from bovine milk whey.
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.
Konecny
P
P
Biotechnology Center, Utah State University, Logan 84322-4700.
Brown
R J
RJ
Scouten
W H
WH
D000327:Adsorption; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D003611:Dairy Products / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D007074:Immunoglobulin G / Q000302:isolation & purification*; D008892:Milk / Q000276:immunology*; D012492:Salts; D013696:Temperature
D007074:Immunoglobulin G; D012492:Salts