Identification of yolk platelet-associated hydrolases in the oocytes of Rhodnius prolixus

Archives of Insect Biochemistry and Physiology
R H NussenzveigHatisaburo Masuda

Abstract

The yolk platelets from Rhodnius prolixus, a blood-sucking bug, are composed mostly of vitellin and here are shown to contain at least two hydrolytic enzymes, a phosphatase and a cathepsin D-like proteinase. Both the proteinase and the phosphatase have an acid pH optimum. No hydrolytic activity was observed under alkaline or neutral conditions. Among several proteinase inhibitors tested, only pepstatin could abolish vitellin breakdown in vitro. The proteinase appears to be bound to the yolk platelet membranes. The phosphatase activity, using p-nitrophenyl phosphate as substrate, was enhanced after disruption of the platelet membrane by Triton X-100. This activity could be inhibited by tartrate but not by p-cloromercuribenzoate.

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Related Concepts

Acid Phosphatase
Tissue Membrane
Phosphoric Monoester Hydrolases
Proteinase inhibitors, antifibrinolytic
Enzymes, antithrombotic
Endopeptidases
Tartrate
Proteolytic Enzyme
4-nitrophenylphosphate
Enzymes for Treatment of Wounds and Ulcers

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