Open AccessNicotinic acetylcholine receptor from chick optic lobe.
Author(s) -
Robert I. Norman,
Fuad Mehraban,
Eric A. Barnard,
J. Oliver Dolly
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.4.1321
Subject(s) - acetylcholine receptor , nicotinic agonist , acetylcholine , protein subunit , muscarinic acetylcholine receptor m5 , receptor , cholinergic , alpha 4 beta 2 nicotinic receptor , nicotinic acetylcholine receptor , ganglion type nicotinic receptor , biochemistry , chemistry , medicine , biology , endocrinology , muscarinic acetylcholine receptor m3 , gene
An alpha-bungarotoxin-sensitive nicotinic cholinergic receptor from chick optic lobe has been completely purified. Its standard sedimentation coefficient is 9.1 S. The value near 12 S reported for the related component from other brain regions can be reproduced when the initial extraction is by Triton X-100 (rather than Lubrol PX), but other protein is then complexed with it. A single subunit of apparent molecular weight 54,000 is detected, and this subunit is specifically labeled by bromo-[3H]acetylcholine, but only after disulfide reduction. The same size subunit likewise is labeled in the protein (purified similarly) from the rest of the chick brain which can also bind alpha-bungarotoxin and nicotinic ligands. Immunological crossreactivity is demonstrated between both of these proteins with an antiserum to pure acetylcholine receptor from skeletal muscle. The acetylcholine receptor from chick optic lobe and the alpha-bungarotoxin-binding protein from the rest of the brain appear similar or identical by a series of criteria and are related to (but with differences from) peripheral acetylcholine receptors.