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The Nicotinic Acetylcholine Receptor

Its Structure, Multiple Binding Sites, and Cation Transport Properties

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Part of the book series: New Horizons in Therapeutics ((NHTH))

Abstract

The acetylcholine receptor (AcChR) from Torpedo electroplax has been isolated both in its native membrane-bound state and by affinity chromatography after solubilization (see Conti-Tronconi and Raftery, 1982). Purified membrane fragments can reseal, forming closed, right-side-out vesicles, which can be used for both functional and structural studies. The major physiochemical properties of T. californica AcChR protein are summarized in Fig. 1.

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© 1985 Plenum Press, New York

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Raftery, M.A., Conti-Tronconi, B.M., Dunn, S.M.J., Crawford, R.D., Middlemas, D. (1985). The Nicotinic Acetylcholine Receptor. In: Poste, G., Crooke, S.T. (eds) Mechanisms of Receptor Regulation. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2131-6_15

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  • DOI: https://doi.org/10.1007/978-1-4613-2131-6_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9259-3

  • Online ISBN: 978-1-4613-2131-6

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