Characterization of the β-Adrenergic Receptor and the Regulatory Control of Adenylate Cyclase

  • Alexander Levitzki
Part of the NATO Advanced Study Institutes Series book series (NSSA, volume 11)


Numerous tissues possess β-adrenergic receptors coupled to adenylate cyclase. The binding of 1 -catecholamines to the β-adrenergic receptor is specific, rapid and reversible (5, 16). The extent of receptor occupancy is controlled by the expression
$$ \rm K_D=\ \ {(R)\ \ (H)\over (RH)}\\1 $$
where KD is the receptor-hormone dissociation constant, (R) the concentration of free receptor, (H)the concentration of free hormone and (RH)the concentration of the receptor-hormone complex. The affinity of 1 -catecholamines to the β-receptor as measured by the dose response curve of adenylate cyclase is between 5 × 10−7 M to 10−5 M depending on the activating 1-catecholamine ligand. Since the receptor concentration accessible experimentally rarely exceeds 5 × 10−9 m, attempts to probe the β-receptor by measuring 3H-catacholamine binding were bound to be unsuccessful (6–8). Indeed, it was demonstrated that the ligand binding specificity did not match the specificity of theβ-receptor as defined pharmacologically and biochemically (3, 4). Recent experiments (4, 9) have indeed shown that most of the binding signal is due to non-specific catecholamine binding to non-receptor binding sites. Therefore it became necessary to develop a reliable binding assay for the purpose of direct measurement of ligand binding to the receptor. Such an assay was first developed using 3H-pro-pranolol as the probing ligand (9).


Adenylate Cyclase Adenylate Cyclase Activity Receptor Concentration cAMP Formation Ghost Membrane 
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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Alexander Levitzki
    • 1
  1. 1.Department of Biological ChemistryThe Hebrew University of JerusalemJerusalemIsrael

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