Cleavage of a trypsin chymotrypsin inhibitor from Phaseolus vulgaris in active fragments

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Two peptide fragments can be separated from one of thePhaseolus vulgaris trypsin chymotrypsin inhibitors (PVI 3) after modifying with trypsin and cleaving the disulfide bonds by S-sulfonation. Reogidation of the larger C-terminal fragment yields a polypeptide with chymotrypsin-inhibitory activity. — After incubation with chymotrypsin two different behaving fragments are obtained from PVI 3 by treatment as described above. The now larger N-terminal fragment inhibits after reogidation trypsin and chymotrypsin, and this reogidation gives chymotrypsin-inhibitory activity for the C-terminal fragment, too.