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THE SECRETORY CYCLE OF DIONAEA MUSCIPULA ELLIS IV. THE ENZYMOLOGY OF THE SECRETION
Author(s) -
ROBINS R. J.,
JUNIPER B. E.
Publication year - 1980
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1980.tb01681.x
Subject(s) - secretion , proteases , protease , iodoacetamide , biochemistry , chemistry , alkylation , enzyme , biology , cysteine , catalysis
S ummary 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.