Hydrophilic interaction liquid chromatography coupled with LC- MS/MS was used to analyze the crude venom extracts of Echis ocellatus (Carpet viper) and Bitis arietans (Puff adder). The gel-free proteomic analysis of the crude venom extracts from E. ocellatus and B. arietans yielded the identification of 86 and 80 proteins, respectively. Seventy- nine proteins were common between the two snake species with a 90.8% similarity. The identified proteins belong to 12 protein families where serine proteases (22.31%) and metalloproteinases (21.06%) were the dominant proteins in the venom of B. arietans. Metalloproteinases (34.84%), phospholipase A 2 s (25.69%) and serine proteases (17.25%) represents the major toxins in the E. ocellatus venom. This study provides some valuable insights into the toxin families to be neutralized in case of envenomation.