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Atropine dissociates complexes of muscarinic acetylcholine receptor and guanine nucleotide‐binding protein in heart membranes
Author(s) -
Matesic Diane F.,
Luthin Gary R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80680-2
Subject(s) - muscarinic acetylcholine receptor , atropine , guanine , muscarinic acetylcholine receptor m5 , chemistry , membrane , nucleotide , acetylcholine receptor , acetylcholine , muscarinic acetylcholine receptor m3 , muscarinic acetylcholine receptor m2 , biochemistry , biophysics , receptor , pharmacology , endocrinology , biology , gene
Complexes of muscarinic acetylcholine receptor and guanine nucleotide‐binding protein (G protein) are formed in the presence of the agonist carbachol. The complexes remain stable after removal of agonist, and survive subsequent solubilization from cardiac membranes and purification. Dissociation of the receptor from the G protein occurs when the antagonist atropine is added following removal of agonist. This is the first direct demonstration of destabilization of receptor—G protein complexes by the binding of an antagonist.