Purification of toxic peptides and the amino acid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae:Ctenidae).

The venom of the wandering spider Cupiennius salei was analysed biochemically by gel filtration, cation exchange chromatography, RP-HPLC, IEF, SDS-PAGE and TLC-electrophoresis. The native venom contains high levels of Na+, K+, Ca2+, histamine and taurine. It shows considerable activity of hyaluronidase, but not proteolytic activity. Thirteen peptides (CSTX-1 to CSTX-13) with an apparent mol. wt between 2.6 and 12.5 kDa causing differently strong toxic, effects were purified. Toxicity data of the crude venom (insects and mouse) are given and compared with the toxicity of CSTX-1, which causes most of the crude venom's toxicity. CSTX-1 has a mol. wt of 8352.6 and its amino acid sequence of 74 amino acids is given.