Antibodies against an alpha-bungarotoxin-binding peptide of the alpha-subunit of the acetylcholine receptor.
Polyclonal and monoclonal antibodies were raised against a peptide comprising residues 173-204 of the alpha-subunit of the acetylcholine receptor. The polyclonal and pooled monoclonal antibodies inhibited up to 50% of 125I-alpha-bungarotoxin binding to peptide 173-204. Some of the antibodies recognized native receptor but did not significantly affect alpha-bungarotoxin binding. Epitope mapping revealed that the antibodies are directed against residues 183-194 indicating this region is a major determinant of toxin binding. This region is most likely conformationally constrained in the native receptor.
Donnelly-Roberts
D L
DL
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Lentz
T L
TL
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D001667:Binding, Competitive; D015153:Blotting, Western; D002038:Bungarotoxins / Q000378:metabolism*; D000939:Epitopes / Q000276:immunology*; D046911:Macromolecular Substances; D051379:Mice; D008807:Mice, Inbred BALB C; D010446:Peptide Fragments / Q000276:immunology* / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000276:immunology* / Q000378:metabolism; D014101:Torpedo
D000906:Antibodies; D000911:Antibodies, Monoclonal; D002038:Bungarotoxins; D000939:Epitopes; D046911:Macromolecular Substances; D010446:Peptide Fragments; D011950:Receptors, Cholinergic