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  Selective photoaffinity labeling of acetylcholine receptor using a cholinergic analogue

Witzemann, V., & Raftery, M. A. (1977). Selective photoaffinity labeling of acetylcholine receptor using a cholinergic analogue. Biochemistry, 16(26), 5862-5868. doi:10.1021/bi00645a034.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-2B04-B Version Permalink: https://hdl.handle.net/21.11116/0000-0001-2B05-A
Genre: Journal Article

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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 bisazido derivative was synthesized from bis(3-aminopyridinium)-1,10-decane diiodide and it was shown that it was bound (KD congruent to 2.2 muM) specifically to purified acetylcholine receptor and fulfilled the requirements for a photoaffinity label. Like the parent compound the derivative could transform membrane-bound receptor from a low ligand affinity conformation(s) to a high ligand affinity form (s), a transition which is thought to resemble desensitization processes observed in vivo. Photolysis of 3H-labeled bisazido reagent was carried out in the presence of the receptor. After dodecyl sulfate-polyacrylamide gel electrophoresis of labeled purified receptor two of the four subunits (mol wt 40 000 and 60 000) contained 90% of the bound radioactivity while for membrane-bound receptor the subunits of mol wt 40 000 and 50 000 were labeled. The results favor the assumption that the specific ligand binding sites are located on mol wt 40 000 subunits and labeling of the other subunits reflects (a) their proximity to the ligand-binding site and (b) alterations in subunit topography between membrane-bound and solubilized states.

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Language(s): eng - English
 Dates: 1977-07-0619771977-12-27
 Publication Status: Issued
 Pages: 7
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 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi00645a034
URI: https://www.ncbi.nlm.nih.gov/pubmed/588561
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 16 (26) Sequence Number: - Start / End Page: 5862 - 5868 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103