Please use this identifier to cite or link to this item: https://repository.unej.ac.id/xmlui/handle/123456789/112685
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dc.contributor.authorOKTARIANTI, Rike-
dc.contributor.authorSUHARDIANSYAH, Alfan-
dc.contributor.authorERNI, Elisa-
dc.contributor.authorWATHON, Syubbanul-
dc.contributor.authorSENJARINI, Kartika-
dc.date.accessioned2023-03-13T02:31:05Z-
dc.date.available2023-03-13T02:31:05Z-
dc.date.issued2023-
dc.identifier.urihttps://repository.unej.ac.id/xmlui/handle/123456789/112685-
dc.description.abstractApyrase 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%.en_US
dc.language.isoenen_US
dc.publisherAtlantis Pressen_US
dc.subjectApyraseen_US
dc.subject56 kDa immunogenic proteinen_US
dc.subjectAedes aegyptien_US
dc.titleThe Apyrase Functional Properties of the 56 kDa Protein from Aedes Aegypti Salivary Glanden_US
dc.typeArticleen_US
Appears in Collections:LSP-Conference Proceeding



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