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

Rike Oktarianti; Alfan Suhardiansyah; Elisa Erni; Syubbanul Wathon; Kartika Senjarini

doi:10.2991/978-94-6463-062-6_14

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

Authors

Rike Oktarianti¹, Alfan Suhardiansyah¹, Elisa Erni¹, Syubbanul Wathon¹, Kartika Senjarini¹^{, *}

¹Biology Department, Faculty of Mathematics and Natural Sciences, University of Jember, Jember, 68121, Indonesia

^*Corresponding author. Email: senjarini@unej.ac.id

Corresponding Author

Kartika Senjarini

Available Online 22 December 2022.

DOI: 10.2991/978-94-6463-062-6_14 How to use a DOI?
Keywords: Apyrase; 56 kDa immunogenic protein; Aedes aegypti
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%.
Copyright: © 2023 The Author(s)
Open Access: Open Access This chapter is licensed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/), which permits any noncommercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

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Volume Title: Proceedings of the 4th International Conference on Life Sciences and Biotechnology (ICOLIB 2021)
Series: Advances in Biological Sciences Research
Publication Date: 22 December 2022
ISBN: 10.2991/978-94-6463-062-6_14
ISSN: 2468-5747
DOI: 10.2991/978-94-6463-062-6_14 How to use a DOI?
Open Access: Open Access This chapter is licensed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/), which permits any noncommercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

Cite this article

ris enw bib

TY  - CONF
AU  - Rike Oktarianti
AU  - Alfan Suhardiansyah
AU  - Elisa Erni
AU  - Syubbanul Wathon
AU  - Kartika Senjarini
PY  - 2022
DA  - 2022/12/22
TI  - The Apyrase Functional Properties of the 56 kDa Protein from Aedes aegypti Salivary Gland
BT  - Proceedings of the 4th International Conference on Life Sciences and Biotechnology (ICOLIB 2021)
PB  - Atlantis Press
SP  - 135
EP  - 143
SN  - 2468-5747
UR  - https://doi.org/10.2991/978-94-6463-062-6_14
DO  - 10.2991/978-94-6463-062-6_14
ID  - Oktarianti2022
ER  -

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