Biochemical and Immunological Methods to Purify the β-Adrenergic Receptors

  • A. D. Strosberg
Part of the Methodological Surveys in Biochemistry and Analysis book series (MSBA, volume 13)


Two approaches have been used to purify the β-adrenergic catecholamine receptor from turkey erythrocyte plasma membranes. The biochemical method involves the preparation of an affinity gel containing alprenolol, a potent β-adrenergic antagonist, coupled to agarose, through a ‘spacer arm’. Affinity chromatography of digitonin-solubilized membranes yielded a 20,000-fold purified receptor which had conserved essentially all the pharmacological properties of the membrane-bound binding sites. Adenylate cyclase was not retained on this affinity gel [1]. Two-dimensional electrophoresis revealed the presence of two major components of mol. wts. corresponding to 70,000 and 60,000, and two minor components of mol. wts. 33,000 and 30,000 [2].


Dopamine Receptor Adenylate Cyclase Muscarinic Receptor Senior Editor Catecholamine Receptor 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • A. D. Strosberg
    • 1
  1. 1.Molecular Immunology Laboratory, Institut Jacques Monod (IRBM)CNRS - Université Paris VIIParisFrance

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