Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion.
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.
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts.
J A
JA
DeBin
J E
JE
Maggio
G R
GR
Strichartz
D000595:Amino Acid Sequence; D000818:Animals; D003400:Astacoidea / Q000187:drug effects; D018118:Chloride Channels; D002851:Chromatography, High Pressure Liquid; D003058:Cockroaches / Q000187:drug effects; D008024:Ligands; D008297:Male; D008565:Membrane Proteins / Q000187:drug effects / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012604:Scorpion Venoms / Q000378:metabolism* / Q000494:pharmacology
D018118:Chloride Channels; D008024:Ligands; D008565:Membrane Proteins; D010455:Peptides; D012604:Scorpion Venoms; C091539:Chlorotoxin