A modified nicotinic acetylcholine receptor lacking the 'ion channel amphipathic helices'.
Antibodies to a synthetic peptide from the 'amphipathic helix' of the alpha-chain of the nicotinic acetylcholine receptor (nAChR) bound both to detergent-solubilised and membrane-bound nAChR, indicating that this region, suggested as a component of the transmembrane ion channel in one model, is not buried in the membrane. Trypsinisation of membranes prior to affinity purification yielded preparations lacking the amphipathic helices of the alpha- and beta-chains and probably also of the gamma- and delta-chains. Such material should allow direct testing, by reconstitution experiments, of the importance of these regions for channel activity.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D001666:Binding Sites, Antibody; D002462:Cell Membrane / Q000378:metabolism; D004557:Electric Organ / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera / Q000276:immunology; D007118:Immunoassay; D007473:Ion Channels / Q000378:metabolism*; D008970:Molecular Weight; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000276:immunology / Q000378:metabolism*; D014101:Torpedo / Q000378:metabolism*; D014357:Trypsin
D000911:Antibodies, Monoclonal; D007106:Immune Sera; D007473:Ion Channels; D011978:Receptors, Nicotinic; D014357:Trypsin