Multiple binding states of muscarinic acetylcholine receptors in membranes from neuroblastoma X glioma hybrid cells

William L. Klein*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Membranes of neuron-like NG108-15 hybrid cells bind [3H]quinuclidinyl benzilate (QNB) with high affinity and specificity. Greater than 90% of total [3H]QNB binding is to sites having the pharmacological specificity of muscarinic acetylcholine receptors. Three significant features characterize the interaction of ligands with these sites: (1) Specific binding of [3H]QNB at equilibrium follows a simple adsorption isotherm with an apparent KD of 1 × 10-10 M; (2) Rates of [3H]QNB association and dissociation are biphasic and, as the binding reaction proceeds, the fraction of readily dissociable [3H]QNB decreases; (3) Competition against [3H]QNB for specific binding sites by antagonists gives a slope of 1 when analyzed on Hill plots, but competition for binding sites by agonists gives a slope of less than 1. A simple two-step model for activation is proposed to account for these features.

Original languageEnglish (US)
Pages (from-to)1058-1066
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume93
Issue number4
DOIs
StatePublished - Apr 29 1980

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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