Purification and characterization of chlorotoxin, a chloride channel ligand from the venon 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 blocki...

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Bibliographic Details
Published inThe American journal of physiology Vol. 264; no. 2
Main Authors DeBin, J.A. (Harvard Medical School, Boston, MA), Maggio, J.E, Strichartz, G.R
Format Journal Article
LanguageEnglish
Published 01.02.1993
Subjects
CHLORURE
CLORUROS
ION
IONES
PEPTIDE
PEPTIDOS
PURIFICACION
PURIFICATION
SCORPIONES
SISTEMA NERVIOSO
SYSTEME NERVEUX
TOXICIDAD
TOXICITE
TOXINAS
TOXINE
VENENOS
VENIN
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Summary: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
Bibliography:L50
9401685
ISSN:0002-9513
2163-5773