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Journal Article

Agonist-activated ionic channels in acetylcholine receptor reconstituted into planar lipid bilayers


Sakmann,  Bert
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Boheim, G., Hanke, W., Barrantes, F. J., Eibl, H., Sakmann, B., Fels, G., et al. (1981). Agonist-activated ionic channels in acetylcholine receptor reconstituted into planar lipid bilayers. Proceedings of the National Academy of Sciences of the United States of America, 78(6), 3586-3590. Retrieved from http://www.pnas.org/content/78/6/3586.

Cite as: https://hdl.handle.net/21.11116/0000-0000-F679-3
Planar lipid bilayers were formed with the mixed chain phospholipid 1-stearoyl-3-myristolglycero-2-phosphocholine. Acetylcholine receptor membrane fragments or the purified receptor protein was incorporated into these bilayers by fusing receptor-containing vesicles with the planar membranes a few degrees below the lipid phase transition temperature. Single-channel currents activated by nicotinic agonists in the reconstituted system resembled those observed in intact rat and frog muscle membrane as measured by the patch clamp technique. The observed channel characteristics did not depend on the degree of receptor purification. Thus, the receptor-enriched fragments and those depleted of nonreceptor peripheral peptides, the purified receptor monomer/dimer mixtures, and the isolated receptor monomer as defined by gel electrophoresis all shared similar electrochemical properties in the synthetic lipid bilayer. The agonist-activated ionic channel seems, therefore, to be contained within the receptor monomer.