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Media type:
E-Article
Title:
Reconstitution of Functional Membrane-Bound Acetylcholine Receptor from Isolated Torpedo californica Receptor Protein and Electroplax Lipids
Contributor:
Gonzalez-Ros, J. M.;
Paraschos, A.;
Martinez-Carrion, M.
Published:
National Academy of Sciences of the United States of America, 1980
Published in:
Proceedings of the National Academy of Sciences of the United States of America, 77 (1980) 4, Seite 1796-1800
Language:
English
ISSN:
0027-8424
Origination:
Footnote:
Description:
Purified acetylcholine receptor and total lipids, both extracted from Torpedo californica electroplax, were utilized to reconstitute chemically excitable membrane vesicles. Reconstitution was achieved by dialysis of the extraction detergent, octyl β -D-glucoside, from protein/lipid incubation mixtures. The reconstituted preparations could be fractionated by sucrose density gradient centrifugation and consisted of vesicular structures visible in electron micrographs. In addition, the reconstituted vesicles exhibited the following properties characteristic of native receptor-enriched membranes: (i) an external distribution of α -bungarotoxin-binding sites, (ii) a time-dependent binding of α -bungarotoxin that is depressed by preincubation with the cholinergic agonist carbamoylcholine (``desensitization''), (iii) an ability to retain22Na+that is lost in the presence of detergents or gramicidin A, and (iv) a carbamoylcholine-induced acceleration of22Na+efflux that can be blocked by α -bungarotoxin. The purified acetylcholine receptor that was utilized in the reconstitution experiments apparently does not require other protein components for ligand recognition or ion translocation.