ISOLATION OF SOYBEAN HEMAGGLUTININ AND DEMONSTRATION OF MULTIPLE FORMS BY ISOELECTRIC FOCUSING

Soybean (Glycine max) hemagglutinin was isolated from soybean whey protein by isoelectric focusing in the region between pH 5 and pH 8. Four different forms of the protein designated A, B, C, and D were separated and their isoelectric points were determined to be at pH 5.85, pH 6.00, pH 6.10, and pH 6.20, respectively. The four hemagglutinins were shown to be immunochemically identical. The major hemagglutinin (form B) was isolated in homogeneous form as judged by disc electrofocusing, disc electrophoresis, and immunoelectrophoresis. Dissociation of hemagglutinin B in the solvent system phenol-acetic acid-0.2 m mercaptoethanol (2:1:1, w/v/v) made 5 m in urea resulted in the separation of two subunits as indicated by disc electrophoresis in the same solvent. © 1969.