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|Title:||Isolation and pharmacological characterization of cannitoxin, a presynaptic neurotoxin from the venom of the papuan taipan (Oxyuranus scutellatus canni)|
|Source:||Kuruppu, S., Reeve, S., Banerjee, Y., Kini, R.M., Smith, A.I., Hodgson, W.C. (2005-12). Isolation and pharmacological characterization of cannitoxin, a presynaptic neurotoxin from the venom of the papuan taipan (Oxyuranus scutellatus canni). Journal of Pharmacology and Experimental Therapeutics 315 (3) : 1196-1202. ScholarBank@NUS Repository. https://doi.org/10.1124/jpet.105.093641|
|Abstract:||The Papuan taipan (Oxyuranus scutellatus canni) is widely distributed throughout much of Papua New Guinea. Although neurotoxicity is a major symptom of envenomation, no neurotoxins have been isolated from this venom. Using a series of size exclusion chromatography steps, we report the isolation of cannitoxin, a presynaptic neurotoxin (44,848 Da) that represents approximately 16% of the whole venom. The toxin displayed high phospholipase A2 (PLA2) activity (330 ± 5 μmol/ min/mg) and caused concentration-dependent (11-66 nM) inhibition of indirect (0.2 ms; 0.1 Hz; supramaximal V) twitches of the chick biventer cervicis nerve-muscle preparation without effecting nicotinic receptor agonists. Prior addition of CSL Taipan antivenom (5 U/ml) or inhibition of phospholipase A2 activity by incubation with 4-bromophenacyl bromide prevented the inhibition of twitches. Cannitoxin is composed of three different subunits, α, β, and γ, with the possibility of two β isomers. However, only the α subunit displayed in vitro neurotoxic activity of its own. Thus, cannitoxin is similar in structure and pharmacology to taipoxin, which has been isolated from the closely related Australian species O. scutellatus scutellatus (coastal taipan). Copyright © 2005 by The American Society for Pharmacology and Experimental Therapeutics.|
|Source Title:||Journal of Pharmacology and Experimental Therapeutics|
|Appears in Collections:||Staff Publications|
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