MAJOR PH 4.5 SOLUBLE PROTEINS OF SOYBEAN COTYLEDONS .I. SEPARATION BY GEL FILTRATION, DISC ELECTROFOCUSING AND IMMUNOELECTROPHORESIS

1. 1.Disc electrofocusing was used successfully in the separation and approximate estimation of the isoelectric points of the major components of the pH 4.5 soluble proteins of soybean cotyledons. 2. 2.Some of the major components were identified as Kunitz trypsin inhibitor, lipoxidase, and multiple hemagglutinins. 3. 3.The pH 4.5 soluble proteins were separated into six fractions by Sephadex G-100 gel filtration. The soybean glycoproteins (hemagglutinins) were eluted in one fraction. 4. 4.The components of each gel filtration fraction were analyzed by disc electrofocusing and immunoelectrophoresis by using rabbit antisera to the unfractionated pH 4.5 soluble proteins. 5. 5.It was observed that the major components followed a pattern of decreasing molecular size being associated with lower isoelectric points. © 1969.