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 bioche mically by gel filtration, cation exchange chromatography, RP-HPLC, IE F, SDS-PAGE and TLC-electrophoresis. The native venom contains high le vels of Na+, K+, Ca2+, histamine and taurine. It shows considerable ac tivity of hyaluronidase, but no proteolytic activity. Thirteen peptide s (CSTX-1 to CSTX-13) with an apparent mol. wt between 2.6 and 12.5 kD a causing differently strong toxic effects were purified. Toxicity dat a of the crude venom (insects and mouse) are given and compared with t he 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 ami no acids is given.