Agonist-specific alterations in receptor binding affinity associated with solubilization of turkey erythrocyte membrane beta adrenergic receptors

L. J. Pike, R. J. Lefkowitz

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

The beta adrenergic receptor binding sites of turkey erythrocyte membranes, identified by (-)-[3H]dihydroalprenolol binding, were solubilized with digitonin. The binding sites in particulate and soluble preparations displayed appropriate characteristics of beta1 adrenergic specificity, stereospecificity, high affinity and saturability. The affinity of all agonists tested was significantly (2-50-fold) greater in the soluble than in the particulate preparations. The affinities of antagonists, however, were identical in the soluble and particulate preparations. Agonist-specific alterations in receptor binding affinity were also found to be mediated by assay temperature. Thus agonist but not antagonist affinities increased as the temperature was lowered from 37° to 4°. Possible molecular mechanisms responsible for the observed shifts are discussed.

Original languageEnglish
Pages (from-to)370-375
Number of pages6
JournalMolecular pharmacology
Volume14
Issue number2
StatePublished - Jan 1 1978
Externally publishedYes

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