The Apyrase Functional Properties of the 56 kDa Protein from Aedes aegypti Salivary Gland

Abstract

Apyrase is an enzyme an inhibit platelet aggregation process, capa ble of degrading ADP in the process blood feeding and mostly found in hematophagous arthropods. While vector’s blood feeding, this apyrase salivary protein is responsible for inhibiting platelet aggregation in the human host, by hydrolyzing adenosine diphosphate or adenosine triphosphate molecules that pro duce adenosine monophosphate thus decrease platelet aggregation. Our previ ous study reported that the immunogenic proteins 56 kDa from salivary gland of dengue’s vector Aedes aegypti constituted high apyrase activity. This study wanted to analyze apyrase functional properties of this immunogenic protein. The amount of inorganic phosphate released from ADP degradation by apyrase was analyzed using by malachite green detection kit. We also further analyzed its platelet aggre gation inhibition activity. The results showed that 56 kDa immunogenic protein has high apyrase activity with 33.30 nmol/well inorganic phosphate released, half of positive control activity (ATP-se) and it can inhibit platelet aggregation by in vitro was 40–50%.