ABSTRACTSoybean (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 wi