Abstract
Ultracentrifugation resolved water-extractable soybean proteins into four fractions of 2S, 7S, 11S, and 15S. Chromatography on hydroxylapatite with potassium phosphate gradients (0.03–0.5 M) at pH 7.6 yielded four major fractions, A, B, C, and D. Fraction A was eluted with the starting buffer (0.03 M); the other fractions were eluted under influence of the gradient. Ultracentrifugal compositions in decreasing order of relative amounts were Fraction A, 2S; Fraction B, 2S and 7S; Fraction C, 11S, 7S, 15S, and 2S; and Fraction D, 7S, 11S, and 15S. Soybean protein fractions also chromatographed included isoelectrically precipitated globulins, whey proteins, cold-insoluble fraction, crystalline trypsin inhibitor, and hemagglutinin.
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