Strang_1989_Neurosci.Lett_104_201

Polyclonal antibodies were produced in rabbits to propylbenzilylcholine mustard-bovine serum albumin (PBCM-BSA) conjugates. The antibodies selectively recognized and bound to an apparent single class of sites with high affinity for PBCM. The antibodies also demonstrated high to intermediate affinity for muscarinic ligands which have benzhydryl or dicyclohexane ring structures similar to PBCM. The antibodies had little or no affinity for ligands which lacked the double cyclohexane structure. Antibodies recognized muscarinic receptors specifically labeled with [3H]PBCM, but not unlabeled receptors, on immunoblots. These results suggest that the polyclonal antibodies produced in this study react specifically with the dicyclohexane structure on PBCM and that this antigenic determinant remains available for interaction with the antibodies, even when the ligand is bound to the receptor.