Chromatographic purification of immunoglobulin G from bovine milk whey

We used thiophilic chromatography on T-gel, a resin of the structure agarose-O-CH 2CH 2SO 2CH 2 CH 2SCH 2CH 2OH, 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...

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Bibliographic Details
Published inJournal of Chromatography A Vol. 673; no. 1; pp. 45 - 53
Main Authors Konecny, Premysl, Brown, Rodney J., Scouten, William H.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.07.1994
Subjects
Adsorption
Animals
Chromatography, Affinity - methods
Dairy Products - analysis
Electrophoresis, Polyacrylamide Gel
Immunodiffusion
Immunoglobulin G - isolation & purification
Milk - immunology
Salts
Temperature
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Summary:We used thiophilic chromatography on T-gel, a resin of the structure agarose-O-CH 2CH 2SO 2CH 2 CH 2SCH 2CH 2OH, 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.
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SourceType-Scholarly Journals-1
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ISSN:0021-9673
DOI:10.1016/0021-9673(94)87056-X