Antibodies against an α-bungarotoxin-binding peptide of the α-subunit of the acetylcholine receptor

Abstract

Polyclonal and monoclonal antibodies were raised against a peptide comprising residues 173-204 of the α-subunit of the acetylcholine receptor. The polyclonal and pooled monoclonal antibodies inhibited up to 50% of 125I-α-bungarotoxin binding to peptide 173-204. Some of the antibodies recognized native receptor but did not significantly affect α-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. © 1989.