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Affinity directed crosslinking of acetylcholine receptor polypeptide components in post-synaptic membranes

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://www.sciencedirect.com/science/article/pii/0006291X78912081/pdf?md5=5ea09b6d4fe134687c550f8a1c866a8b&pid=1-s2.0-0006291X78912081-main.pdf
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https://doi.org/10.1016/0006-291X(78)91208-1
(beliebiger Volltext)

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Zitation

Witzemann, V., & Raftery, M. A. (1978). Affinity directed crosslinking of acetylcholine receptor polypeptide components in post-synaptic membranes. Biochemical and Biophysical Research Communications, 85(2), 623-631. doi:10.1016/0006-291X(78)91208-1.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-24B2-D
Zusammenfassung
A photolabile derivative of α-bungarotoxin which binds specifically to acetylcholine receptor has been used to investigate the topography of the membrane associated protein. It is shown that the toxin can be crosslinked to a polypeptide of 40,000 daltons, to which it is known to bind, and in addition to another polypeptide of 65,000 daltons which is a major constituent of the membrane. The results substantiate the notion that this nicotinic acetylcholine receptor is composed of different polypeptides and that some of these interact with each other or are in close proximity on the exterior surface of the post-synaptic membrane.