Purification and partial characterization of a ‘short' insectotoxin‐like peptide from the venom of the scorpion Parabuthus schlechteri

FEBS Letters

Müller, Gert J.¹  Daenens, Paul⁴  Debont, Tom⁴  Possani, Lourival D.⁵  van der Walt, Jurg J.²  Rostoll, Karin²  Verdonck, Fons³  Tytgat, Jan⁴ 

[1] Department of Pharmacology, University of Stellenbosch, P.O. Box 19063, Tygerberg 7505, South Africa;Department of Physiology, University of Potchefstroom, Private Bag x6001, Potchefstroom 2520, South Africa;Interdisciplinary Research Center, University of Leuven Campus Kortrijk, B-8500 Kortrijk, Belgium;Laboratory of Toxicology, University of Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium;Instituto de Biotecnologı́a, UNAM, Avenida Universidad 2001, Cuernavaca, Morelos 62250, Mexico

关键词: Scorpion;    Venom;    Toxin;    Peptide;    Insectotoxin;    Parabuthus;   

DOI  :  10.1016/S0014-5793(98)01589-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A disulfide-rich, low-molecular-mass toxin-like peptide has been isolated from Parabuthus schlechteri venom using gel filtration, ion exchange, and reversed phase chromatography. Partial characterization of this peptide reveals a relationship with four-disulfide bridge proteins belonging to the family of ‘short' insectotoxins (44% residue identity). In recognition hereof, the peptide was named PBITx1 (sITx10). Our work also reports on the deduced sequences of two other ‘short' insectotoxins from Buthus eupeus, I₃ and I₄, and it provides a consensus sequence and nomenclature for all known ‘short' insectotoxins. Finally, sequence similarities with K⁺ channel blockers (charybdotoxin, κ-conotoxin), and a Cl⁻ channel blocker (chlorotoxin) are highlighted.

【 授权许可】

Unknown