Abstract
1. 1. By use of specific synthetic substrates and inhibitors, trypsin and chymotrypsin have been demonstrated in the digestive tracts of both sexes of adult Carabus taedatus and Calosoma calidum. 2. 2. No evidence for carboxypeptidase-A, carboxypeptides-B or aminopeptidase was found. 3. 3. At 30°C the trypsin has a pH optimum at pH 8·2–8·3. 4. 4. The trypsin has been partially purified and its molecular weight estimated by Sephadex G-100 column chromatography to be approximately 20,000–23,000. 5. 5. The trypsin is inhibited by TLCK, PMSF, 2-mercapto-ethanol, human and porcine serum.
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