Abstract
There is both high-affinity and low-affinity nicotinic cholinergic binding of [ 3H]acetylcholine ([ 3H]ACh) in rat brain membrane preparations. As determined by a filtration binding assay, [ 3H]ACh bound with K d =36.0±8.4 nM and B max = 19.4±4.5 fmol/mg protein or 3.3±0.7 fmol/mg tissue for high-affinity binding and K d about 10 −7 to 10 −6 M and B max about 6–10 fmol/mg tissue or 40–60 fmol/mg protein for low-affinity binding. d-Tubocurarine (1 mM) inhibits high- as well as low-affinity binding, whereas 10 μM α-bungarotoxin does not compete at both binding sites. Substance P had no effect on the binding parameters of high-affinity nicotinic cholinergic binding.
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