Proteomic analysis identifies diverse toxins in Acanthophis antarcticus venom, indicating important functional roles.
Key Points
Acanthophis antarcticus venom displays notable fibrinogenolytic and serine peptidase inhibitory activities, expanding its functional profile.
Nine toxin families were identified through advanced techniques such as LC-MS/MS, highlighting three-finger toxins and phospholipase A2 as predominant.
Functional assessments confirmed the activity of key enzymes, including HYAL, PLA2, and LAAO, adding new insights to venom composition.
These findings underscore the biochemical diversity of Acanthophis antarcticus venom, indicating its potential implications in toxin research.