1983•Cold Spring Harbor Symposia on Quantitative BiologyRequires access
The Nicotinic Acetylcholine Receptor: Subunit Structure, Functional Binding Sites, and Ion Transport Properties
Michael A. Raftery, Susan M. J. Dunn, Bianca Maria Conti-Tronconi, David S. Middlemas, Rebecca D. Crawford
Open publisher page 31 citations
Abstract
The acetylcholine receptor (AChR) from Torpedo electroplax can be isolated in a pure form either in its native membrane-bound state or by affinity chromatography after solubilization. This is due to very dense packing of the AChR molecules in the postsynaptic membrane that excludes other intrinsic membrane components. Purified membrane fragments can reseal, forming closed, right-side-out vesicles, which can be used for functional and structural studies of the AChR.