Isolation and Characterization of the Protein That Co-Purifies With Soybean (Glycine Max L.) Glycinin

Soybean (Glycine max. L.) glycinin (11S) purified by the Thanh and Shibasaki method (J. Agric. Food Chem. 24, 1117–1121 (1976)) is usually 90% pure. One of the impurities present in such glycinin preparations is the sulfur-rich salt-soluble globulin (SRP). The SRP which co-purifies with glycinin is resolved when such glycinin preparations are chromatographed on a DEAE DE-53 anionexchange column. It represented up to 5.32% of the total protein recovered. Hydrophobic and disulfide exchange interactions are the likely forces responsible for the co-purification of SRP with glycinin.