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• W2037582982 abstract "High-affinity, specific binding of radiolabeled α-bungarotoxin to particulate fractions derived from rat brain shows saturability (Bmax ≈ 37fmol/mg, KDapp = 1.7 nM) and insensitivity to ionic strength, and is essentially irreversible (Kon = 5 · 106 min−1 · mol−1; Kdisplacement = 1.9 · 10−4 min−1, τ1/2 = 62 h). Subcellular distribution of specific sites is consistent with their location on synaptic junctional complex and post-synaptic membranes. These membrane-bound binding sites exhibit unique sensitivity to cholinergic ligands; pretreatment of membranes with cholinergic agonists (but not antagonists) induces transformation of α-bungarotoxin binding sites to a high affinity form toward agonist. The effect is most marked for the natural agonist, acetylcholine. These results strongly support the notion that the entity under study is an authentic nicotinic acetylcholine receptor." @default.
• W2037582982 created "2016-06-24" @default.
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• W2037582982 date "1978-12-01" @default.
• W2037582982 modified "2023-09-26" @default.
• W2037582982 title "α-Bungarotoxin binding properties of a central nervous system nicotinic acetylcholine receptor" @default.
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• W2037582982 doi "https://doi.org/10.1016/0304-4165(78)90098-3" @default.
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