EC-PIII, a novel non-hemorrhagic procoagulant metalloproteinase: Purification and characterization from Indian Echis carinatus venom.

Procoagulant snake venom toxins find extensive use as reagents in laboratory tests and diagnostic kits. In the present study we report a novel P-III class procoagulant SVMP, EC-PIII from Echis carinatus venom. EC-PIII was purified using a combination of gel-filtration and anion-exchange chromatography. It has a molecular mass of 110kDa and is a dimeric protein as determined by SDS-PAGE. DLS results show that the protein is homogenous and stable in solution. Peptide mass fingerprinting revealed that the peptides obtained show high homology to the other members of SVMP family. The enzymatic studies revealed that EC-PIII shows protease activity and is inhibited by metalloproteinase inhibitors such as EDTA. EC-PIII exhibits procoagulant effect under in-vitro conditions. Local toxicity studies revealed that EC-PIII is devoid of hemorrhagic as well as myotoxic activities. This is the first report of a non-hemorrhagic SVMP to be identified from Indian Echis carinatus venom. EC-PIII can find potential use in diagnostic and other therapeutic uses owing to its biochemical and pharmacological properties.