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Functional Equivalence of Monomeric and Dimeric Forms of Purified Acetylcholine Receptors from Torpedo californica in Reconstituted Lipid Vesicles

1980; Wiley; Volume: 109; Issue: 2 Linguagem: Inglês

10.1111/j.1432-1033.1980.tb04819.x

1432-1033

Robert R. H. Anholt, Jon Lindstrom, M Montal,

Free Radicals and Antioxidants

European Journal of BiochemistryVolume 109, Issue 2 p. 481-487 Free Access Functional Equivalence of Monomeric and Dimeric Forms of Purified Acetylcholine Receptors from Torpedo californica in Reconstituted Lipid Vesicles Robert ANHOLT, Robert ANHOLT Receptor Biology Laboratory, Salk Institute for Biological Studies. P.O. Box 1809, San Diego, California, USA 92112Search for more papers by this authorJon LINDSTROM, Jon LINDSTROM Receptor Biology Laboratory, Salk Institute for Biological Studies. P.O. Box 1809, San Diego, California, USA 92112Search for more papers by this authorMauricio MONTAL, Mauricio MONTAL Departments of Biology and Physics, University of California at San Diego, La Jolla, USA 92093Search for more papers by this author Robert ANHOLT, Robert ANHOLT Receptor Biology Laboratory, Salk Institute for Biological Studies. P.O. Box 1809, San Diego, California, USA 92112Search for more papers by this authorJon LINDSTROM, Jon LINDSTROM Receptor Biology Laboratory, Salk Institute for Biological Studies. P.O. Box 1809, San Diego, California, USA 92112Search for more papers by this authorMauricio MONTAL, Mauricio MONTAL Departments of Biology and Physics, University of California at San Diego, La Jolla, USA 92093Search for more papers by this author First published: August 1980 https://doi.org/10.1111/j.1432-1033.1980.tb04819.xCitations: 57AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Acetylcholine receptors from Torpedo californica electric organ were solubilized and purified under conditions which prevent inactivation of the agonist-regulated cation channels. The dimer form of the receptors was preserved during purification. Treatment with reducing agents converted dimers into monomers. Receptor monomers and dimers were separately reconstituted into soybean lipid vesicles by the cholate dialysis technique. Reconstituted monomers and dimers were functionally equivalent with respect to their carbamylcholine-induced dose-dependent uptake of 22Na+, the total flux of 22Na+ per receptor during the permeability response, and the occurrence of desensitization. Evidence against non-covalent association of monomers to produce dimeric functional units was obtained using glutaraldehyde as a crosslinking agent. These results show that both the acetylcholine-binding sites and the agonist-regulated cation-specific channel are contained within the α2βγδ subunit structure of the acetylcholine receptor monomer. Citing Literature Volume109, Issue2August 1980Pages 481-487 ReferencesRelatedInformation