Cereal Chem 44:645 - 652.  |  VIEW ARTICLE
Purification of the 11S Component of Soybean Protein.

A. C. Eldridge and W. J. Wolf. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

Solubilities of the 2S, 7S, 11S, and 15S components in the cold-insoluble fraction of soybean protein were determined in sodium acetate-sodium chloride buffers at pH 4.6, 0-2 C. Solubility of some components varied considerably with ionic strength. Extraction of the cold-insoluble fraction at 25 C. with pH 4.6, 0.5 ionic strength buffer, followed by cooling to 0-2 C., yielded 3-4 mg. protein per ml. having a composition of 8, 21, and 70% for the respective 2S, 7S, and 11S components. When these solubles were diluted to pH 4.6, 0.3 ionic strength and cooled to 0-2 C., a precipitate formed. The precipitate contained 5-8% 7S component and 92-95% 11S component; it was devoid of 2S and 15S material. Further fractionation of this precipitate on Sephadex G-200 resulted in an 11S fraction which appeared to be homogeneous.