Michaelson, Daniel M. and Raftery, Michael A. (1974) Purified acetylcholine receptor: Its reconstitution to a chemically excitable membrane. Proceedings of the National Academy of Sciences of the United States of America, 71 (12). pp. 4768-4772. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:MICpnas74
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Association of purified acetylcholine receptor from Torpedo californica electroplax with lipids from the same organism results in a vesicular membrane system in which the receptor protein is oriented so that all neurotoxin binding sites appear to be on the outer surface. The reconstituted system is chemically excitable by acetylcholine and carbamylcholine, as measured by 22Na+ efflux. This excitability is specifically blocked by the antagonist α-bungarotoxin. These results demonstrate that the purified receptor macromolecule contains not only the specific neurotransmitter binding site but also the molecular elements necessary for ion translocation in order to effect postsynaptic depolarization.
|Additional Information:||© 1974 by the National Academy of Sciences. Communicated by Jerome Vinograd, September 18, 1974. This research was supported by grants from the National Institute of Health (USPHS-NS-10294) and from the Sloan Foundation. M.A.R. was a recipient of a Research Career Development Award. We wish to thank Dr. George Rouser for help with analysis of Torpedo lipids and Dr. Ken Reed for development of the 22Na efflux assay. Church Laboratory of Chemical Biology, Contribution No. 4947.|
|Subject Keywords:||acetylcholine binding; ion translocation|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||21 Feb 2007|
|Last Modified:||14 Nov 2014 19:19|
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