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Binding of Agonists and Antagonists to Muscarinic Acetylcholine Receptors on Intact Cultured Heart Cells
Author(s) -
Nathanson Neil M.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb00862.x
Subject(s) - agonist , muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m5 , carbachol , receptor , binding site , chemistry , quinuclidinyl benzilate , muscarinic acetylcholine receptor m3 , acetylcholine , muscarinic acetylcholine receptor m1 , acetylcholine receptor , muscarinic agonist , muscarinic acetylcholine receptor m2 , biochemistry , biology , endocrinology
The binding of agonists and antagonists to muscarinic acetylcholine receptors on intact cultured cardiac cells has been compared with the binding observed in homogenized membrane preparations. The antagonists [ 3 H]quinuclidinyl benzilate and [ 3 H] N ‐methylscopolamine bind to a single class of receptor sites on intact cells with affinities similar to those seen in membrane preparations. In contrast with the heterogeneity of agonist binding sites observed in membrane preparations, the agonist carbachol binds to a homogeneous class of low‐affinity sites on intact cells with an affinity identical to that found for the low‐affinity agonist site in membrane preparations in the presence of guanyl nucleotides. Kinetic studies of antagonist binding to receptors in the absence and presence of agonist did not provide evidence for the existence of a transient (> 30 s) high‐affinity agonist site that was subsequently converted to a site of lower affinity. Nathanson N. M . Binding of agonists and antagonists to muscarinic acetylcholine receptors on intact cultured heart cells.