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The physical and chemical properties of γ-conglycinin of soybean (Glycine max) were investigated. The soybean protein extracted from soybean meal using 0.2M NaCl solution at pH 4.5 was passed through a Sephadex G-150 column to isolate 7S globulin γ-Conglycinin was isolated and purified from the 7S globulin with a DEAE Sephadex A-50 column chromatagraphy. The protein preparation was pure on immunoelectrophoresis, polyacrylamide gei electrophoresis and gel isoelectric fouling. It had an isoelectric point at ph 5.4 and contained 16.12% nitrogen 4.18% mannose and 1.215 glucosamine. Amino acid composition, in general, shaved that γ-conglycinin contained higher contents of lysine, dicarboxylic acids and ammonia nitrogen, and lower contents of sulfur-contsining amino acids and tryptophan. The subunits of γ-conglycinin were distributed in the range of pH 4.6-5.5. The subunits located in the pH region of 4.6-5.0 and 5.0-5.5 were glycopeptides (molecular weight of 38,000) and simple peptide (MW of 32,000), respectively.
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