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. 1974 Jul;71(7):2773–2776. doi: 10.1073/pnas.71.7.2773

The Binding Characteristics and Number of β-Adrenergic Receptors on the Turkey Erythrocyte

Alexander Levitzki 1,*, Daphne Atlas 1, Michael L Steer 1,†
PMCID: PMC388553  PMID: 4528016

Abstract

Turkey erythrocyte ghosts (empty membranes) possess a class of receptors that can bind both L-[3H]isoproterenol and DL-[3H]propranolol. The binding of [3H]isoproterenol to these receptors occurs with a dissociation constant of 0.15 μM and can be fully inhibited by 1 μM propranolol. The binding of [3H]propranolol occurs with a dissociation constant of 2.5 nM and can be fully inhibited by 0.2 mM DL-isoproterenol. Ligand binding is sensitive to sonication, boiling, and 8 M urea. The cells possess 500 to 1000 β-adrenergic receptors per cell. Binding of propranolol to the β-receptor was found to be stereospecific for the L stereoisomer. If one assumed a 1:1 relationship between β-adrenergic receptors and adenylate cyclase, the turnover number of this adenylate cyclase would be close to 100 min-1.

Keywords: β-receptors, isoproterenol, propranolol, equilibrium dialysis, ultracentrifugation

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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