First report of the characterization of a snake venom apyrase (Ruviapyrase) from Indian Russell’s viper (Daboia russelii) venom
peer-reviewed · International Journal of Biological Macromolecules · 2018
| Date | 2018-05-01 |
| Type | peer-reviewed |
| Venue | International Journal of Biological Macromolecules |
| Publisher | Elsevier BV |
| Contribution | downstream-application |
| DOI | 10.1016/j.ijbiomac.2018.01.038 |
| Citations (OpenAlex) | 9 |
| Venue 2-year citedness | 8.99 |
Abstract
A novel apyrase from Russell’s viper venom (RVV) was purified and characterized, and it was named Ruviapyrase (Russell’s viper apyrase). It is a high molecular weight (79.4 kDa) monomeric glycoprotein that contains 2.4% neutral sugars and 58.4% N-linked oligosaccharides and strongly binds to Concanavalin A. The LC-MS/MS analysis did not identify any protein in NCBI protein database, nevertheless some de novo sequences of Ruviapyrase showed putative conserved domain of apyrase superfamily. Ruviapyrase hydrolysed adenosine triphosphate (ATP) to a significantly greater extent (p -1 , respectively with a turnover number (Kcat) of 24,600 min -1 . Spectrofluorometric analysis demonstrated interaction of Ruviapyrase with ATP and ADP at Kd values of 0.92 nM and 1.25 nM, respectively. Ruviapyrase did not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibited marginal anticoagulant and strong antiplatelet activity, and dose-dependently reversed the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase was significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom.
Methods and tools
- Russell’s viper apyrase (Ruviapyrase): Purifies a novel apyrase from Daboia russelii venom whose identity rested on de novo sequences carrying apyrase domains.
Methods it uses
- PEAKS: Commercial DP-based de novo