Allosteric Properties of the Acetylcholine Receptor Protein from Torpedo marmorata
- J.-P. Changeux*,
- F. Bon‡,
- J. Cartaud†,
- A. Devillers-Thiéry*,
- J. Giraudat*,
- T. Heidmann*,
- B. Holton*,
- H.-O. Nghiêm*,
- J.-L. Popot*,§,
- R. Van Rapenbusch‡, and
- S. Tzartos*
- *Neurobiologie Moléculaire, Institut Pasteur et Laboratoire associé Interactions Cellulaires et Moléculaires du C.N.R.S., Paris, 75015 France; †Laboratoire de Microscopie Electronique, Institut Jacques Monod, Université Paris VII, Paris, 75005 France; ‡Laboratoire de Biologie Structurale, Institut Jacques Monod, Université Paris VII, Paris, 75005 France
This extract was created in the absence of an abstract.
Excerpt
Since the initial characterization of the acetylcholine receptor (AChR) in crude extracts of fish electric organ (Changeux et al. 1970a,b; Miledi et al. 1971; Meunier et al. 1971a,b, 1972a,b; Raftery et al. 1971; Reiter et al. 1972), knowledge about this important regulatory protein developed in an exceptionally fast manner (for review, see Changeux 1981; Conti-Tronconi and Raftery 1982; Anholt et al. 1983). It has been established that the basic unit, or light form, of the AChR consists of four different polypeptide chains of exact molecular weight: α (50,116), β (53,681), γ (56,279), and δ (57,565) (Noda et al. 1982, 1983a,b) in a 2.1.1.1. stoichiometry (Reynolds and Karlin 1978; Lindstrom et al. 1979; Raftery et al. 1980; Saitoh et al. 1980). In extracts of adult Torpedo electric organ, the receptor protein primarily occurs in a species of higher molecular weight or heavy form (Raftery et al. 1972) that results from the...
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↵§ Present address: Yale University, Department of Molecular Biophysics and Biochemistry, New Haven, Connecticut 06511.
