Abstract
End-group analysis of the Bowman-Birk inhibitor which had been exposed to catalytic levels of chymotrypsin (EC 3.4.4.5) at pH 3.8 indicated the cleavage of a Leu-Ser bond. Performic acid oxidation of the chymotrypsin-modified inhibitor yielded two fragments which could be separated by gel filtration on Sephadex G-25. From the end groups and amino acid composition of these two fragments, the chymotrypsin-reactive site was identified as Leu-48 and Ser-49. As in the case of the trypsin-reactive site, the sequence of amino acids in the vicinity of the chymotrypsin-reactive site of the Bowman-Birk inhibitor bears a high degree of homology with the corresponding site of the lima bean inhibitor.
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