Binding of alpha-bungarotoxin to chick sympathetic ganglia: properties of the receptor and its rate of appearance during developement.

Studies were carried out on the binding of [125I]alpha-bungarotoxin (alphaBT) to membrane fragments of chick sympathetic ganglia. Specific binding of toxin was saturable with a KD of 1.1 nM. The rates of association and dissociation of the toxin from ganglionic membranes were 4.3 X 10(4) M-1 sec-1 and 4.6 X 10(-5) sec-1 (t 1/2 = 4.2 h). respectively. Binding was inhibited (by up to 95%) by low concentrations of nicotinic, but not by a muscarinic cholinergic ligand. The properties of the ganglionic binding site for alphaBT were consistent with its being a nicotinic acetylcholine receptor. The development of toxin receptors in chick ganglia was also studied. From days 7 to 11 in ovo, few receptors were present; from days 12 to 20 in ovo, there was a 10-fold increase in receptor number per ganglion; from hatching to maturity, the receptor number per ganglion slowly increased and reached a maximum of 14 fmoles. The ontogeny of receptors for alphaBT in sympathetic ganglia appears to correlate with the cytological maturation and innervation of the principal neurons.