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. 1969 Aug;63(4):1239–1246. doi: 10.1073/pnas.63.4.1239

COMPARED EFFECTS OF DITHIOTHREITOL ON THE INTERACTION OF AN AFFINITY-LABELING REAGENT WITH ACETYLCHOLINESTERASE AND THE EXCITABLE MEMBRANE OF THE ELECTROPLAX*

Thomas Podleski 1, Jean-Claude Meunier 1, Jean-Pierre Changeux 1
PMCID: PMC223456  PMID: 5260926

Abstract

p-(trimethyl ammonium) benzene diazonium difluoroborate (TDF), an affinity-labeling reagent of the acetylcholine receptor site(s), which in the normal cell acts as an irreversible inhibitor becomes a reversible activator after in vivo exposure of the electroplax to dithiothreitol (DTT), a disulfide bond reducing agent. After in vitro exposure of acetylcholinesterase to DTT, TDF becomes a reversible competitive inhibitor of the enzyme, using indophenyl acetate as the substrate. Both acetylcholinesterase and the macromolecular receptor of acetylcholine thus contain disulfide bonds. Additional experiments with DTT suggest that there might exist several different classes of receptor sites for cholinergic agents in the excitable membrane of the electroplax.

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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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