Abstract
1. 1. A chymotrypsin inhibitor of the silkworm haemolymph was purified by ammonium sulphate fractionation, column chromatographies on DEAE-Sephacel, Ultrogel AcA54 and Con A-Sepharose 4B, and chromatofocusing. 2. 2. The purified inhibitor gave a single protein and inhibitor band on polyacrylamide gel electrophoresis. 3. 3. The inhibitor had a mol. wt of approx. 43,000 and an isoelectric point of 5.06, and its inhibitory activity was not affected appreciably by pH 4.5–9.0. 4. 4. The kinetic analysis showed that this inhibitor inhibits chymotrypsin noncompetitively. 5. 5. The inhibitor suppressed not only α-chymotrypsin but also main digestive fluid protease-6B3 from the silkworm and fungal protease from Aspergillus melleus. 6. 6. However, no inhibition of trypsin was detected.
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