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

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

J A DeBin  1 , J E Maggio, G R Strichartz
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Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion (VSports)

J A DeBin et al. Am J Physiol. 1993 Feb.

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 VSports手机版. 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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