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Interaction between beta-adrenergic receptors and guanine-nucleotide sites in turkey erythrocyte-membranes

Academic Article
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Overview

authors

  • Vauquelin, G.
  • Bottari, S.
  • Andre, C.
  • Jacobsson, B.
  • Strosberg, Donny

publication date

  • 1980

journal

  • Proceedings of the National Academy of Sciences of the United States of America-Biological Sciences  Journal

abstract

  • beta 1-Adrenergic receptors from turkey erythrocyte membranes have been identified by specific binding of the radiolabeled antagonist (-)-[3H]dihydroalprenolol. These receptors are inactivated by the alkylating agent N-ethylmaleimide when occupied by beta-adrenergic agonists but not when occupied by antagonists or when unoccupied. A time-dependent decrease of the number of receptor sites is observed. Inactivation affects 45-60% of the sites, regardless of the agonist or N-ethylmaleimide concentration. The guanine nucleotides GTP and 5'-guanylyl imidodiphosphate effectively protect the receptors against agonist-mediated inactivation by N-ethylmaleimide. Protection by ATP necessitates a 100-fold higher concentration; 10 mM NaF is ineffective. The guanine nucleotide effect is reversible and occurs via interaction with N-ethylmaleimide-insensitive sites. These observations establish that guanine nucleotide sites interact with and caused structural modification of the agonist-occupied beta-adrenergic receptors in turkey erythrocyte membranes.

subject areas

  • Allosteric Regulation
  • Animals
  • Erythrocyte Membrane
  • Erythrocytes
  • Ethylmaleimide
  • Fluorides
  • Guanine Nucleotides
  • Protein Conformation
  • Receptors, Adrenergic
  • Receptors, Adrenergic, beta
  • Turkeys
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Identity

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.77.7.3801

PubMed ID

  • 6253990
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Additional Document Info

start page

  • 3801

end page

  • 3805

volume

  • 77

issue

  • 7

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