Reference

Caeruleotoxin: identification in the venom of Bungarus fasciatus, molecular properties and importance of phospholipase A2 activity for neurotoxicity

Caeruleotoxin: identification in the venom of Bungarus fasciatus, molecular properties and importance of phospholipase A2 activity for neurotoxicity. Bon, C.; Saliou, B. (Unite Venins, Inst.In this study， 9001-84-7 and 58205-95-1 are also used. Pasteur, Paris 75015, Fr.). Toxicon, 21(5), 681-98 (English) 1983. CODEN: TOXIA6. ISSN: 0041-0101. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Caeruleotoxin (I) [58205-95-1] was identified and purified from 5 samples of B. fasciatus venom. I was not detected in B. multicinctus or B. caeruleus venoms. By comparing the protein compn. of the venom originally used to purify I with that of venoms of various Bungarus species, it was concluded that original venom was from B. fasciatus but was mislabeled as B. caeruleus venom. Purified I is a slightly basic protein with an isoelec. point of 7.4 which possesses a significant phospholipase A2 [9001-84-7] activity (200 mmol lecithin hydrolyzed/min/mg) and a high lethal potency (i.v. LD50 in mice 0.33-0.07 mg/kg). I is composed of 2 identical subunits of 13,000 mol. wt. which resemble pancreas and snake venom phospholipases in their amino acid compn. 58205-95-1 is the cas registry number of certain chemical which is used as reagents here. Like crotoxin, I irreversibly blocks the postsynaptic response of Torpedo and Electrophorus electrophaques to cholinergic agonists without preventing the binding of acetylcholine to its receptor. By hydrolyzing crit. lipids of the postsynaptic membrane, I stabilizes the acetylcholine receptor-ionophore assembly in a desensitized state. ..