Abstract
A subtilisin inhibitor was purified from the seeds of Canavalia lineata by ammonium sulfate precipitation, ultrafiltration on a YM-30 membrane, column chromatography on DEAE-Toyopearl and SP-Toyopearl, followed by reverse-phase HPLC. The inhibitor (CLSI-I) is a low molecular weight protein (M(r) about 6500) containing no half-cystine residue, and quite stable as to extreme heat and pH treatment. CLSI-I inhibited subtilisin-type serine proteases including S. griseus alkaline protease. The amino acids of CLSI-I were sequenced by manual Edman degradation after enzymatic digestion with Achromobacter lyticus lysyl endopeptidase and Staphylococcus aureus V8 protease. CLSI-I contains 65 amino acid residues and showed a high homology to potato inhibitor I family proteins.
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