Please use this identifier to cite or link to this item: https://repository.unej.ac.id/xmlui/handle/123456789/112685
Title: The Apyrase Functional Properties of the 56 kDa Protein from Aedes Aegypti Salivary Gland
Authors: OKTARIANTI, Rike
SUHARDIANSYAH, Alfan
ERNI, Elisa
WATHON, Syubbanul
SENJARINI, Kartika
Keywords: Apyrase
56 kDa immunogenic protein
Aedes aegypti
Issue Date: 2023
Publisher: Atlantis Press
Abstract: Apyrase is an enzyme an inhibit platelet aggregation process, capable 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 produce adenosine monophosphate thus decrease platelet aggregation. Our previous 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 aggregation 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%.
URI: https://repository.unej.ac.id/xmlui/handle/123456789/112685
Appears in Collections:LSP-Conference Proceeding



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