AJP - Cell Physiology, Vol 264, Issue 2 C361-C369, Copyright © 1993 by American Physiological Society

ARTICLES

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

J. A. DeBin, J. E. Maggio and G. R. Strichartz
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts.

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.

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