Two affinity states of M1 muscarine receptors
- 1 June 1988
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Neurobiology
- Vol. 8 (2) , 181-191
- https://doi.org/10.1007/bf00711244
Abstract
The binding of oxotremorine-M to M1 muscarine receptors was examined by measuring competition between the agonist and3H-pirenzepine, using rabbit hippocampal membranes suspended in 20 mM Tris buffer containing 1 mM Mn2+. Both ligands interacted with a single class of receptors. The receptors could assume two affinity states for oxotremorine-M, with equal numbers of high-affinity (K H) and low-affinity (K L) sites. K H interconverted reversibly toK L in the absence of divalent cations and interconverted reversibly to a state similar toK L in the presence of guanyl 5′-yl imidodiphosphate. The results are compatible with a model in which a model in which a pair of receptor molecules can be stabilized by a guanine nucleotide-binding “G protein” and have one site each ofK H andK L affinity.This publication has 29 references indexed in Scilit:
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