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. 1972 Dec;69(12):3634–3637. doi: 10.1073/pnas.69.12.3634

Partial Characterization of a Tetrodotoxin-Binding Component from Nerve Membrane

Theodore I Benzer 1, M A Raftery 1
PMCID: PMC389837  PMID: 4509325

Abstract

Tetrodotoxin from Japanese puffer fish has been labeled with tritium and purified from the crude mixture obtained. The interaction between the purified [3H]tetrodotoxin and membrane suspensions from the olfactory nerve of long-nosed garfish has been investigated by equilibrium dialysis. Tetrodotoxin binds to membrane suspensions with a dissociation constant KD = 8.3 nM. The nerve preparation binds 42 pmol of [3H]tetrodotoxin/g of wet tissue at saturating toxin concentrations. With various hydrolytic enzymes, the binding component is shown to be a protein embedded in a phospholipid environment. The binding is inhibited below pH 4.0 and is not stable towards heat. Tetrodotoxin binding is not inhibited by the local anesthetic, procaine.

Keywords: garfish olfactory nerve, membrane-bound protein, excitable ion channels

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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