An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

GOMEZ, G; B NERLI; LLEIVA, L.; ACOSTA, G; G, PICÓ

JOURNAL OF VENOMOUS ANIMALS AND TOXINS INCLUDING TROPICAL DISEASES

CEVAP-UNESP

Año: 2012 vol. 18 p. 306 - 316

1678-9199

Snake venoms are rich sources of active proteins that have been employed in the diagnosis andtreatment of health disorders and antivenom therapy. Developing countries demand fast economicaldownstream processes for the purification of this biomolecule type without requiring sophisticatedequipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneouslyprotease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-steppartition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gelfiltration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increasedproteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins