@article {708,
	title = {First report of the characterization of a snake venom apyrase (Ruviapyrase) from Indian Russell{\textquoteright}s viper (Daboia russelii) venom. [Mass Spectromety Facility - Proteomics]},
	journal = {Int J Biol Macromol},
	volume = {111},
	year = {2018},
	month = {2018 Jan 08},
	pages = {639-648},
	abstract = {<p>A novel apyrase from Russell{\textquoteright}s viper venom (RVV) was purified and characterized, and it was named Ruviapyrase (Russell{\textquoteright}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 \&lt; .05) as compared to adenosine diphosphate (ADP); however, it was devoid of 5{\textquoteright}-nucleotidase and phosphodiesterase activities. The Km and Vmax values for Ruviapyrase towards ATP were 2.54 μM and 615 μM of Pi released min-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.</p>
},
	issn = {1879-0003},
	doi = {10.1016/j.ijbiomac.2018.01.038},
	author = {Kalita, Bhargab and Patra, Aparup and Jahan, Shagufta and Mukherjee, Ashis K}
}
