Abstract
Two protease inhibitors were isolated from the plasma of Locusta migratoria and sequenced. They were 35 and 36 amino acids long and revealed very little similitude for the protease inhibitors isolated from other arthropods. They inhibit the proPhenoloxidase Phenoloxidase proteolytic activation cascade in hemocyte extracts of the same insect. This inhibiting activity resulted in a lower production of PO, a key enzyme for the defence mechanism in arthopods. Both peptides however showed a strong in vitro inhibiting activity toward α-chymotrypsin and elastase, LMCI I inhibits the human leukocyte enzyme while LMCI II mostly the pancreatic one, a difference explainable on the basis of the active site sequence changes.
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