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Protease inhibitor controls prophenoloxidase activation in Manduca sexta
Author(s) -
Saul Steven J.,
Sugumaran Manickam
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81543-5
Subject(s) - prophenoloxidase , manduca sexta , hemolymph , serine protease , manduca , biochemistry , biology , protease , protease inhibitor (pharmacology) , proteases , benzamidine , sphingidae , kunitz sti protease inhibitor , trypsin , enzyme , innate immune system , immunology , insect , botany , receptor , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
Prophenoloxidase from the hemolymph of tobacco hornworm Manduca sexta can be activated by a specific activating enzyme found in the cuticle. Inhibition studies with benzamidine, diisopropyl phosphofluoridate and p ‐nitrophenyl‐ p ′‐guanidinobenzoate indicate that the activating enzyme is a trypsin‐like serine protease. An endogenous protease inhibitor, isolated from the hemolymph of Manduca larvae, inhibits the prophenoloxidase activation mediated by this enzyme. These results indicate that the probable physiological role of endogenous protease inhibitor is to control the undesired activation of prophenoloxidase in the hemolymph.