Abstract
We have previously described the purification of a tetrodotoxin binding protein from the electroplax of Electrophorus electricus . The preparation consisted of three peptides of M r ∼ 46,000, 59,000 and ∼ 300,000 daltons. Further investigation has now shown that the large peptide of M r ∼ 260,000 daltons is part of the tetrodotoxin binding component of the voltage-sensitive sodium channel.
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