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Gloydius venom is a rich natural source of proteins possessing platelet aggregation inhibition activity. These proteins or their recombinant analogs are universal instruments for the investigation of proteins and receptors interaction in hemostatic system. At the same time previously studied and potentially new pharmacological properties of platelet aggregation inhibitors from snake venoms create a background for the development of the manufacturing technologies. This study presents a part of technological development of several target proteins parallel obtaining from G. blomhoffii brevicaudus snake venom, in particular deve­lop­ment of manufacturing steps for platelet aggregation inhibitor.The target protein was purified using three different chromatographic approaches. It was shown that it is a single chain protein with molecular weight 12001.55 Da, isoelectrical point 8.03, which inhibited platelet aggregation in the rabbit platelet rich plasma with ID50 = 3.26×10-6 g or 542×10-9 М and revealing no enzyme activity.

Phospholipases A2 (PlA2) are the most common compounds of snake venom. Ability of the enzyme to affect cell interactions, particularly platelet aggregation, proliferation of cancer cells, processes of angiogenesis and cell differentiation, potentiates it as a therapeutic or cancerostatic agent in treatment of malignant tumors. Indicated potential medicinal functions of PLA2 require high purified protein. We developed and probated method for phospholipase A2 obtaining from venom of snake Gloydius blomhoffii brevicaudus. The technology consists of four consecutive stages of chromatographic separation. Purified PLA2 is acidic protein with molecular weight of 13762.86 Dа and рІ 4.17. Estimated optimal pH for the enzyme constitutes 8.5. PLA2 inhibits ADP-induced platelet aggregation and exerts cytotoxic effect. Its ability to induce differentiation of РС12 cells, declared by other authors, was not shown.