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Isolated Adenylate Cyclase and β-Adrenergic Receptor

  • Alma Gal
  • Sergei Braun
  • Hadas Arad
  • Alexander Levitzki
Part of the Methodological Surveys in Biochemistry and Analysis book series (MSBA, volume 13)

Abstract

β-Receptor-sensitive adenylate cyclase can be solubilized in various detergents and partially purified. The partially purified enzyme and the partially purified receptor can be re-incorporated into phospholipid vesicles. The re-constituted β-adrenergic receptor is capable of binding 125I-cyanopindolol, where the affinity for the ligand depends on the phospholipid composition of the vesicle. The hormone sensitivity of the adenylate cyclase is only partially recovered in a full re-constitution assay, most probably because of incomplete functional re-constitution. Achievement of functional re-constitution is the aim of attempts now being made to overcome particular difficulties [1]. We have, however, obtained high-yield re-constitution of the β-receptor with its GTP regulatory unit, and can measure kinetic parameters of the re-constituted system.

Keywords

Adenylate Cyclase Tris Buffer Cyclase Activity Receptor Solubilization Phospholipid Composition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Reference

  1. 1.
    Keenan, A.K., Gal, A. & Levitzki, A. (1982) Biochem. Biophys. Res. Comm. 105, 615–623.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Alma Gal
    • 1
  • Sergei Braun
    • 1
  • Hadas Arad
    • 1
  • Alexander Levitzki
    • 1
  1. 1.Department of Biological Chemistry, Institute of Life SciencesThe Hebrew University of JerusalemJerusalemIsrael

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