An alternative method to isolate protease and phospholipase A2 txins from snake venoms based on aqueous two-phase systems partition

GÓMEZ, GABRIELA; NERLI, BIBIANA; ACOSTA, OFELIA; PICÓ, GUILLERMO; LEIVA, LAURA

JOURNAL OF VENOMOUS ANIMALS AND TOXINS INCLUDING TROPICAL DISEASES

CEVAP-UNESP

Año: 2012

1678-9199

Snake venoms are rich sources of active proteins that have found uses in the diagnosis, treatment of health disorders and antivenom therapy. Developing countries demand fast and economic downstream processes for purification of this kind of bio-molecules without sophisticated equipment requirements. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple step partition procedure with polyethyleneglycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.