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Buchkapitel

Studies on the structure of acetylcholine receptor

MPG-Autoren
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Witzemann,  Veit
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://link.springer.com/content/pdf/10.1007%2F978-1-4684-8643-8_65.pdf
(beliebiger Volltext)

https://doi.org/10.1007/978-1-4684-8643-8_65
(beliebiger Volltext)

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Zitation

Witzemann, V., & Walker, J. H. (1981). Studies on the structure of acetylcholine receptor. In G. Pepeu, & H. Ladinsky (Eds.), Cholinergic Mechanisms. (pp. 653-658). New York: Plenum Press.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-17AC-4
Zusammenfassung
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.