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Differences between detergent-extracted acetylcholine receptor and “cholinergic proteolipid”

Naturevolume 256pages325327 (1975) | Download Citation

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Abstract

SNAKE venom α-toxins1 in combination with reversible2,3 or alkylating4,5 cholinergic ligands give a selective labelling of the cholinergic (nicotinic) receptor protein (AChR)6–8. Since this protein is membrane-bound and therefore expected to possess hydrophobic properties, two different methods have been used for its dissolution and purification: (1) chloroform–methanol extraction9 and (2) non-denaturing detergent extraction in aqueous media2,3. The former solubilises the so-called “cholinergic proteolipid” which, still in organic media, binds charged cholinergic ligands9. The latter procedure has made possible the purification of the AChR by affinity chromatography and the study of the binding of the above-mentioned ligands in physiological media (for reviews see refs 6–8). Furthermore, the serum of rabbits immunised against the purified AChR10–12 blocks in vivo the physiological response to cholinergic agonists10,11, thereby confirming that the detergent-extracted AChR is indeed involved in the permeability change caused by acetylcholine. On the other hand, the physiological importance of the “cholinergic proteolipid” remains undetermined, though the challenge to the actual purification13 has recently been refuted14. It is therefore the aim of the present work to compare the “cholinergic proteolipid” and the detergent-extracted AChR from the same sources: the electric organs of Electrophorus electricus and Torpedo marmorata using the selective labels α-toxin15 and the covalent affinity reagent 4-(N-maleimido)-phenyltrimethylammonium iodide4 in combination with immunodiffusion tests11.

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Author information

Affiliations

  1. Max-Planck Institut für biophysikalische Chemie, 3400, Göttingen-Nikolausberg, West Germany

    • F. J. BARRANTES
  2. Neurobiologie Moléculaire, Institut Pasteur, Paris, France

    • J. P. CHANGEUX
  3. Biochemistry Department, University of Bath, UK

    • G. G. LUNT
  4. Neurobiologie Moléculaire, Institut Pasteur, Paris, France

    • A. SOBEL

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https://doi.org/10.1038/256325a0

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