title: Chemical and pharmacological characterization of toxic polypeptides from the venom of Bungarus caeruleus.
abstract: Five toxic fractions have been purified to homogeneity from the venom of Bungarus ceruleus by chromatography on CM-Sephadex, QAE-Sephadex and Bio-Rex 70 followed by filtration on Sephadex G-50 and Biogel P-30. One of them blocks synaptic transmission at the pre-synaptic level and is identified as a beta-bungarotoxin similar to that described by Lee from the venom of B. multicinctus. Three other ones are short-chain (type I) alpha-toxins which block the response of the isolated electroplaque from Electrophours electricus to bath-applied carbamylcholine. These basic polypeptides of 61-62 amino acids contain four disulfide bridges. A postsynaptically acting toxin, different from the alpha-toxins, has also been purified from the same venom. This ceruleotoxin is acidic and made up of several subunits.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D002038:Bungarotoxins / Q000302:isolation & purification / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D004557:Electric Organ / Q000187:drug effects / Q000502:physiology; D004593:Electrophorus; D008297:Male; D051379:Mice; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology; D012910:Snake Venoms / Q000494:pharmacology; D013569:Synapses / Q000187:drug effects
chemical_list: D000596:Amino Acids; D002038:Bungarotoxins; D010455:Peptides; D012910:Snake Venoms