Endogenous protease inhibitors prevent undesired activation of prophenolase in insect hemolymph.
Phenoloxidase activation in the whole hemolymph of Sarcophaga bullata and Manduca sexta larvae is shown to be achieved by proteolytic cleavage of the proenzyme. This process is inhibited by the serine protease inactivator, Diisopropyl phosphofluoridate. Endogenous protease inhibitors isolated from the larvae inhibit alpha-chymotrypsin mediated prophenoloxidase activation in the hemolymph. These observations suggest that the endogenous protease inhibitors prevent undesired activation of prophenol oxidase in the hemolymph by inhibiting the serine protease involved in the activation process.
D000818:Animals; D004156:Catechol Oxidase / Q000032:analysis*; D002918:Chymotrypsin / Q000494:pharmacology; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000032:analysis*; D006458:Hemolymph / Q000201:enzymology*; D007313:Insecta; D011480:Protease Inhibitors / Q000494:pharmacology*; D012697:Serine Endopeptidases
D004792:Enzyme Precursors; D011480:Protease Inhibitors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D012697:Serine Endopeptidases; D002918:Chymotrypsin