Abstract
Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. 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 polyethylene-glycol/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.
Highlights
Snake venoms are rich sources of bioactive polypeptides and proteins
Aqueous Two-Phase Partitioning Figure 1 shows the partitioning pattern produced by proteins from B. alternatus venom with protease activity corresponding to the overall extraction process
Venom proteins with phospholipase A2 activity exhibited an even distribution among phases at the first extraction step; in the subsequent stages its partitioning equilibrium was displaced to the bottom phase
Summary
Snake venoms are rich sources of bioactive polypeptides and proteins. Some of these components that exhibit enzymatic activities include proteinases, phospholipases A2, nucleotidases, phosphodiesterases and L-amino acid oxidases. Gel filtration, ion-exchange and reversedphase high-pressure liquid chromatography (RP-HPLC) are widely used to purify individual venom proteins [1, 12,13,14]. This methodology is expensive, requires technologically advanced equipment – columns, pumps and matrix – and demands long periods of time
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