PHOSPHOLIPASE A2 PURIFICATION AND CHARACTERIZATION FROM VENOM OF SNAKE GLOYDIUS BLOMHOFFII BREVICAUDUS

A. I. Zhukova, G. L. Volkov, Ye. N. Krasnobryzhaya, S. P. Gavryliuk


DOI: http://dx.doi.org/10.30970/sbi.0601.195

Abstract


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.


Keywords


snake venom, Gloydius blomhoffii brevicaudus, phospholipase A2, liquid chromatography

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