Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion

Am J Physiol. 1993 Feb;264(2 Pt 1):C361-9. doi: 10.1152/ajpcell.1993.264.2.C361.

Abstract

We have previously demonstrated that the venom of the scorpion Leiurus quinquestriatus blocks small-conductance Cl- channels, derived from epithelial cells, when applied to the cytoplasmic surface. We have now purified to near homogeneity, and characterized, the component responsible for this blocking activity. It is a small basic peptide of 4,070 Da. The primary amino acid structure shows considerable homology to a class of previously described putative short insectotoxins. A brief characterization of the kinetics of Cl- channel block as well as a demonstration of toxicity to arthropods is also presented.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Astacoidea / drug effects
  • Chloride Channels
  • Chromatography, High Pressure Liquid
  • Cockroaches / drug effects
  • Ligands
  • Male
  • Membrane Proteins / drug effects
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / isolation & purification*
  • Rats
  • Rats, Sprague-Dawley
  • Scorpion Venoms / metabolism*
  • Scorpion Venoms / pharmacology

Substances

  • Chloride Channels
  • Ligands
  • Membrane Proteins
  • Peptides
  • Scorpion Venoms
  • Chlorotoxin