title: Large scale purification of toxins from the venom of the scorpion Androctonus australis Hector.
abstract: A large scale procedure for purification of the toxins in the venom of the North African scorpion Androctonus australis has been developed. This procedure optimizes the sequence of the steps, leading to better yields of toxins and shortening of the time. It is possible to use 10-15 g batches of venom and also prevent cross-contamination of the toxins. High pressure liquid chromatography has been used to separate AaH I and I', two isotoxins which differ by one amino acid residue in position 17: valine or isoleucine. The procedure allows the characterization of a new toxin active in mice, AaH IV, which represents 0.6 and 2.5% of the venom weight and toxicity, respectively. This new component has been characterized as an alpha toxin made up of 61 amino acid residues and having a neutral isoelectric point.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism; D002845:Chromatography / Q000379:methods; D004589:Electrophoresis, Disc; D007525:Isoelectric Focusing; D007928:Lethal Dose 50; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D012604:Scorpion Venoms / Q000032:analysis*; D014118:Toxins, Biological / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity
chemical_list: D000596:Amino Acids; D012604:Scorpion Venoms; D014118:Toxins, Biological