Abstract
The water-extractable protein and the cold-insoluble fraction prepared from defatted soybean meals were fractionated by the method of gel filtration with Sephadex G-200, resulting in higher purification of the 11S protein and in isolation of the 2S and 7S proteins. Attempts to remove the 7S or 15S contaminant from the 11S protein fraction were successful through the chromatography of calcium phosphate gel. N-terminal analysis of the purified 11S protein allowed deduction that there are three kinds of N-terminal amino acids in it; glycine, phenylalanine, and leucine or isoleucine.
