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Each fragment was separated and purified by gel filtration on Sephadex G\u201050, G\u201075 or G\u2010100, and referred to as fragments A, B, C, and D from the amino\u2010 to the carboxyl\u2010terminal region of the inhibitor.<\/jats:p><jats:p>Soybean trypsin inhibitor (Kunitz) consisted of 181 amino acid residues and its molecular weight was proved to be 20100. Fragments A, B, C, and D consisted of 63, 21, 30, and 67 amino acid residues, respectively. 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