An investigation of the biological activity of bullrout (Notesthes robusta) venom

Bullrout envenomation is known to cause intense pain. Crude bullrout venom and venom fractions were assessed for protease, hyaluronidase, phospholipas e and hemolytic activities, reactivity with stonefish antivenom, lethality to brine shrimp and ability to elicit pain in human subjects. Compared with venom obtained from frozen specimens, live fish venom-milking techniques rendered greater venom potency and improved storage characteris tics. Although mild proteolytic and hemolytic activity was observed, crude venom demonstrated no hyaluronidase or phospholipase A(2) activity, did not affect brine shrimp, or show antigenicity with stonefish antivenom. A sing le venom protein isolated from bullrout venom is attributed with causing pa in in human subjects. The sensations elicited by this novel algesic protein are consistent with chemical stimulation of polymodal nociceptors. (C) 199 9 Elsevier Science Ltd. All rights reserved.