Computer Science
Scientific paper
Aug 1976
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1976pnas...73.2624h&link_type=abstract
Proceedings of the National Academy of Sciences of the United States of America, Volume 73, Issue 8, pp. 2624-2628
Computer Science
3
Scientific paper
Membrane fragments from electric tissue of Torpedo californica containing nicotinic acetylcholine receptor are composed of four different polypeptide chains with molecular weights of 40,000 (α ), 48,000 (β ), 62,000 (γ ), and 66,000 (δ ). The α and β chains are still present in all and γ and δ in some of the receptor preparations after Triton X-100 extraction and purification by affinity chromatography. All components of the receptor react covalently with the photoaffinity label 4-azido-2-nitrobenzyltrimethylammonium fluoroborate, the δ chain incorporating less of the reagent as compared to the α and β chains. Agonists and antagonists containing a quaternary ammonium group protect all chains against the label; the principal neurotoxin from Naja naja siamensis protects the α chain only. We conclude that the α chain binds the neurotoxin from Naja naja, the α and β chains are involved in the binding of ligands with quaternary ammonium groups, and the function of the γ and δ chains remains to be determined.
Bandini G.
Hucho F.
Kiefer H. R.
Layer Paul
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