Abstract
Charybdotoxin, a 37 amino acid peptide isolated from scorpion venom, is a potent inhibitor of potassium channel function. [ 125I]charybdotoxin was originally believed to be a selective ligand for the Ca 2+-sensitive channel in many tissues, but it appears to bind only to a voltage-sensitive potassium channel in brain. We found high densities of [ 125I]charybdotoxin binding in the lateral olfactory tract, interpeduncular nucleus and a variety of mesencephalic nuclei. Moderate levels were found in the cerebral cortex, medial thalamus, hypothalamus and selected thalamic nuclei. These results indicate that [ 125I]charybdotoxin identifies a potassium channel or channels with a unique distribution in the brain.
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