A study of trypsin in Calosoma calidum (FAB.) and Carabus taedatus FAB

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.