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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-24B2-D Version Permalink: https://hdl.handle.net/21.11116/0000-0001-24B3-C
Genre: Journal Article

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BiochemBiophysResComm_85_1979_623.pdf (Any fulltext), 719KB
 
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 Creators:
Witzemann, Veit1, 2, 3, 4, Author           
Raftery, Michael A., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
3Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              
4Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1978-09-0119781978-11-29
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0006-291X(78)91208-1
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Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 85 (2) Sequence Number: - Start / End Page: 623 - 631 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1