The binding characteristics and number of β adrenergic receptors on the turkey erythrocyte

A. Levitzki, D. Atlas, M. L. Steer

Research output: Contribution to journalArticlepeer-review

104 Scopus citations

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. (13 references)

Original languageEnglish
Pages (from-to)2773-2776
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number7
DOIs
StatePublished - 1974
Externally publishedYes

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