Purification and chemical characterization of the major toxins from the venom of the Brazilian scorpion Tityus serrulatus Lutz and Mello

Abstract

The soluble venom from the Brazilian scorpion Tityus serrulatus Lutz and Mello was fractionated on Sephadex G-50 followed by ion exchange chromatography in carboxymethyl-cellulose, resolving at least 10 different toxic components. In this communication the purification and chemical characterization of four major components is reported. The toxins were found to be single polypeptide chains with molecular weights of approximately 7,000, 61-63 amino acid residues and four disulphide bridges. Amino terminal sequence determination of these toxins after reduction and alkylation revealed three unique sequences up until residue fourty-one. For toxin II-11 (14) and toxin III-10 the N-terminal sequence is: Lys-Glu-Gly-Tyr-Leu-Met-Asp-His-Glu-Gly-Cys-Lys-Leu-Ser-Cys-Phe-Ile-Arg-Pro-Ser-Gly-Tyr-Cys-Gly-Arg-Glu-Cys-Gly-Ile-Lys-Lys-Gly-Ser-Ser-Gly-Tyr-Cys-Ala-Trp-Pro. Toxin III-8 has the following N-terminal sequence: Lys-Glu-Gly-Tyr-Ala-Met-Asp-His-Glu-Gly-Cys-Lys-Phe-Ser-Cys-Phe-Ile-Arg-Pro-Ala-Gly-Phe-Cys-Asp-Gly-Tyr-Cys-Lys-Thr-His-Leu-Lys-Ala-Ser-Ser-Gly-Tyr-Cys-Ala-Trp-Pro. Toxin IV-5 has the N-terminal sequence: Lys-Lys-Asp-Gly-Tyr-Pro-Val-Glu-Tyr-Asp-Asn-Cys-Ala-Tyr-Ile- Cys-Trp-Asn-Tyr-Asp-Asn-Ala-Tyr-Cys-Asp-Lys-Leu-Cys-Lys-Asp-Lys-Lys-Ala-Asp-Ser-Gly-Tyr-Cys-Tyr-Trp-Val. © 1981 Carlsberg Laboratory.