Immunological distinction between acetylcholine receptor and the alpha-bungarotoxin-binding component on sympathetic neurons.

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Abstract
Clone PC12 of a rat sympathetic neuron cell line bounds .alpha.-bungarotoxin and exhibited carbamoylcholine-stimulated uptake of Na+. Concentrations of .alpha.-bungarotoxin that saturated the .alpha.-bungarotoxin-binding site had no effect on agonist-stimulated Na+ uptake. Antibodies against eel acetylcholine receptor blocked the agonist-induced Na+ flux but failed to recognize the .alpha.-bungarotoxin-binding component. Detergent extracts of the PC12 clone inhibited the ability of antibody to eel acetylcholine receptor to recognize 125I-.alpha.-bungarotoxin-acetylcholine receptor complexes derived from muscle. These results distinguished between a ganglionic nicotinic acetylcholine receptor and an .alpha.-bungarotoxin-binding component on these cells, and provided evidence for antigenic similarities between muscle acetylcholine receptor and ganglionic acetylcholine receptor.