The Secretory Cycle of Dionaea Muscipula Ellis Iv. The Enzymology of the Secretion

Summary The proteolytic activity of the secretion is examined using inhibitors and site‐specific substrates. The major protease present is not peptic, tryptic or chymotryptic, but may be a thiol protease as activity is inhibited by alkylation with iodoacetamide. Acetylation causes an inhibition of activity, suggesting that one of the major proteases may have an amide group involved in its action. Carboxypeptidase A is found to be present. The secretion is shown to contain chitinolytic and peroxiditic activities but not N‐acetyl‐β‐d‐glucosaminidase. The possible origin of the secretion is discussed.