Snake venom contains a variety of chemicals including pharmacological and toxicological properties. Venom proteins that are enabling such pharmacological properties have not been understood in details yet. We extracted venoms from Indian cobra (Naja naja) and viper (Vipera russelli) and purified by ion-exchange chromatography with DEAE Sephadex A-25 column, followed by HPLC connected with GF-250 column. The highest purification peaks obtained for fraction numbers 3-6 of both snake venoms when elution buffer with 0.1-0.2M NaCl was used in ionexchange chromatography. The purity and molecular mass of the eluted fractions have further analyzed and confirmed by HPLC and SDS-PAGE. These results reported that the purified proteins were low molecular masses ranged from 10-17kD, which resembled to phospholipase A2 of other snake venoms. The potential antibacterial activity of these purified proteins was found against gram negative bacteria like E.coli by agar diffusion assay using 20μl concentrations, suggested these venom proteins can be useful for some pharmacological applications. MALDI-TOF-MS studies will further be helpful to understand the molecular structure of these proteins in detail.