Studies on the Structure of Acetylcholine Receptor

  • V. Witzemann
  • J. H. Walker
Part of the Advances in Behavioral Biology book series (ABBI, volume 25)


The subunit composition of the nicotinic acetylcholine receptor (AChR) from elasmobranch fish is still a matter of controversy. Results obtained from affinity chromatography (6,9), immunology (2,4), crosslinking experiments (10,12) and. labelling studies using photolabile ligands (11,13) support the notion that AChR is composed of more than one polypeptide chain and that the complex of molecular weight (MW) approximately 250,000 Dalton (7) is composed of four different polypeptides of apparent MW 40,000, 50,000, 60,000 and 65,000 Dalton. Nevertheless, other workers report that the 40,000 MW polypeptide chain is the predominant polypetide (3,8) with the other polypeptides present only in trace amounts and copurified with the receptor in a rather irreproducible manner. Using crossed rocket Immunoelectrophoresis with antibodies raised to detergent solubilized, purified AChR from Torpedo californica we present further evidence for the multisubunit structure of the AChR.


Acetylcholine Receptor Nicotinic Acetylcholine Apparent Molecular Weight Subunit Composition Membrane Fragment 
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Copyright information

© Plenum Press, New York 1981

Authors and Affiliations

  • V. Witzemann
    • 1
  • J. H. Walker
    • 1
  1. 1.Abteilung NeurochemieMax-Planck-Institute fur Biophysikalische ChemieGottingenFederal Republic of Germany

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