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Physical Properties of Biological Membranes and Their Functional Implications pp 147–175Cite as

The Acetylcholine Receptor and its Membrane Environment

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Abstract

The nicotinic acetylcholine receptor (AChR) is by far the best characterized neurotransmitter receptor protein. Various disciplines have contributed to our current understanding of this macromolecule: Early biochemical studies were catalyzed by the availability of tissue sources rich in AChR and appropriate ligands like the α-toxins; more recently the application of immunochemistry, cDNA recombinant techniques, rapid kinetic methods and patch-clamp electrophysiological techniques have produced spectacular advances in the field. The AChR is a glycophosphoprotein of about a quarter of a million molecular weight composed of two quasi-identical subunits (α) and three additional chains (β γ, δ) in a mole ratio of 2:1:1:1 (Reynolds and Karlin, 1978; Raftery et at, 1980; Lindstrøm et al, 1982). Apparent molecular weights determined by SDS gel electrophoresis are 39,000,48,000,58,000, and 64,000, respectively, whereas the exact molecular weights predicted from the nucleotide sequences of the cDNAs coding for each subunit are 50,166 (α), 53,681 (β), 56,279(γ), and 57,565 (δ) (Numa et al, 1983). The α subunits carry the recognition site for agonist and competitive antagonists. All subunits are glyco-polypeptides and traverse the membrane at least once.

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  1. Instituto de Investigaciones Bioquímicas (INIBIBB), Universidad Nacional del Sur, C.C. 857, 8000, Bahía Blanca, Argentina

    F. J. Barrantes

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    Cecilia Hidalgo

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Barrantes, F.J. (1988). The Acetylcholine Receptor and its Membrane Environment. In: Hidalgo, C. (eds) Physical Properties of Biological Membranes and Their Functional Implications. Series of the Centro de Estudios Científicos de Santiago. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0935-2_6

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