Identification of the cardiac beta-adrenergic receptor protein: solubilization and purification by affinity chromatography.

Journal Article (Journal Article)

A protein that binds catecholamines with a specificity parallel to that of their in vivo effects on cardiac contractility (isoproterenol > epinephrine or norepinephrine > dopamine > dihydroxyphenylalanine) was solubilized from a microsomal fraction of canine ventricular myocardium. The binding protein was purified 500 to 800-fold by solubilization and subsequent affinity chromatography with conjugates of norepinephrine linked to agarose beads. Purified beta-adrenergic binding protein exists in two forms, corresponding to molecular weights of 40,000 and 160,000. The purified material has a single association constant, 2.3 x 10(5) liters/mol (as compared to two association constants, 10(7) and 10(6) liters/mol, for the binding protein in particulate form) but retains the identical binding specificity for beta-adrenergic drugs and antagonists.

Full Text

Duke Authors

Cited Authors

  • Lefkowitz, RJ; Haber, E; O'Hara, D

Published Date

  • October 1972

Published In

Volume / Issue

  • 69 / 10

Start / End Page

  • 2828 - 2832

PubMed ID

  • 4507606

Pubmed Central ID

  • PMC389654

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.69.10.2828


  • eng

Conference Location

  • United States