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      Determination of the subunit stoichiometry of a voltage-activated potassium channel.

      Nature
      Animals, Charybdotoxin, Membrane Potentials, Membrane Proteins, physiology, Mutation, Potassium Channels, drug effects, genetics, RNA, metabolism, Scorpion Venoms, toxicity, Xenopus

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          Abstract

          The voltage-activated K+, Na+ and Ca2+ channels are responsible for the generation and propagation of electrical signals in cell membranes. The K+ channels are multimeric membrane proteins formed by the aggregation of an unknown number of independent subunits. By studying the interaction of a scorpion toxin with coexpressed wild-type and toxin-insensitive mutant Shaker K+ channels, the subunit stoichiometry can be determined. The Shaker K+ channel is found to have a tetrameric structure. This is consistent with the sequence relationship between a K+ channel and each of the four internally homologous repeats of Na+ and Ca2+ channels.

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