A monoclonal antibody raised against Torpedo nicotinic acetylcholine receptor has been used to study the neurotransmitter binding site of the acetylcholine receptor from several sources. When tested on Torpedo receptor, this monoclonal antibody inhibited binding of alpha-bungarotoxin to 50% of the available sites. The failure to completely inhibit binding of the toxin is attributed to the orientation of the determinant for the monoclonal antibody on the receptor molecule. This monoclonal antibody bound very poorly to the acetylcholine receptor from muscle tissues. This suggests either a modification or a reduced accessibility of the determinant to the monoclonal antibody.
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