Project description:we used a combination of bottom-up (BU) and top-down (TD) proteomics approaches to identify and characterize venom protein compositions of Echis carinatus sochureki (ECS) from three different Iranian populations.
Project description:In order to study the proteome of Echis carinatus carinatus venom of Indian origin, crude venom was fractionated on a Shodex KW-803 gel filtration column coupled to Dionex Ultimate 3000 UHPLC system. The resulting peaks were pooled and subjected to in-solution trypsin digestion and subsequent tandem mass spectrometry analysis. The raw data were then analysed using PEAKS 8.5 software to finally decipher the complex venom proteome.
Project description:In order to study the proteome of Echis carinatus venom from Sri Lanka (SL ECV), crude SL ECV was subjected to 12.5% SDS-PAGE analysis. The resulting SDS-PAGE bands were subjected to in-gel trypsin digestion and subsequent tandem mass spectrometry analysis. The raw data were then analysed using PEAKS 8.5 software to finally decipher the complex venom proteome.
Project description: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.
