Studies on prophenoloxidase activation in the mosquito Aedes aegypti L.
Open Access
- 3 March 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 188 (3) , 507-515
- https://doi.org/10.1111/j.1432-1033.1990.tb15429.x
Abstract
This study, the first of its kind in a mosquito vector species, demonstrates the feasibility of studying prophenoloxidase activation in an insect containing not more than a few microliters of hemolymph. Mosquito phenoloxidase was found to be in an inactive proenzyme form, prophenoloxidase. Mosquito prophenoloxidase required bivalent cation for its activation; Ca2+ was found to be the most efficient for activation. Concomitant amidase activity was also observed prior to phenoloxidase activity. Through Western blotting, using a cross-reactive silkworm anti-prophenoloxidase antibody, our results strongly suggest that mosquito prophenoloxidase activation resulted from limited proteolysis. Protease inhibitor studies reinforced this contention showing the involvement of (a) serine protease(s) with trypsin-like activity in the activation of mosquito prophenoloxidase.This publication has 40 references indexed in Scilit:
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