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. 1984 Aug;82(4):853-61.
doi: 10.1111/j.1476-5381.1984.tb16482.x.

Solubilization and characterization of guanine nucleotide-sensitive muscarinic agonist binding sites from rat myocardium

C P Berrie, N J Birdsall, E C Hulme, M Keen, J M Stockton

Solubilization and characterization of guanine nucleotide-sensitive muscarinic agonist binding sites from rat myocardium

C P Berrie et al. Br J Pharmacol. 1984 Aug.

Abstract

Muscarinic receptors from rat myocardial membranes may be solubilized by digitonin in good yield at low temperatures in the presence of Mg2+. Under these conditions, up to 60% of the soluble receptors show high affinity binding for the potent agonist [3H]-oxotremorine-M (KA = 10(9)M-1), which is inhibited by 5'-guanylylimidodiphosphate. The muscarinic binding site labelled with [3H]-oxotremorine-M has a higher sedimentation coefficient (13.4 s) than sites labelled with a 3H antagonist in the presence of guanylylimidodiphosphate (11.6 s) and probably represents a complex between the ligand binding subunit of the receptor and a guanine nucleotide binding protein.

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References

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    1. Br J Pharmacol. 1984 Aug;82(4):839-51 - PubMed
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