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Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands.

Publication ,  Journal Article
Caron, MG; Srinivasan, Y; Snyderman, R; Lefkowitz, RJ
Published in: Proc Natl Acad Sci U S A
May 1979

Antibodies raised against purified beta-adrenergic receptors themselves specifically bind beta-adrenergic ligands. Digitonin-solubilized frog (Rana pipiens) erythrocyte beta-adrenergic receptors, purified 100- to 200-fold by adsorption to an alprenolol-agarose affinity support and specifically eluted from the affinity resin by 1-100 mM (+/-)-isoproterenol, were used to immunize six rabbits. All immune sera, in contrast to preimmune sera, bound the beta-adrenergic antagonist [(3)H]Dihydroalprenolol binding activity was due to immunoglobulins. By competition studies, antibody [(3)H]dihydroalprenolol binding was found to display a specificity and stereoselectivity resembling that of the beta-adrenergic receptor, [i.e., (-)-isoproterenol > (-)-epinephrine > (-)-norepinephrine; alprenolol approximately propranolol >> phentolamine = aloperidol; and (-) isomers of both agonists and antagonists 10-100 times more potent than (+) isomers]. A portion of the [(3)H]dihydroalprenolol binding antibodies could be specifically adsorbed onto purified frog erythrocyte membranes, whereas Xenopus and human erythrocyte membranes, both of which are almost devoid of beta-adrenergic receptors, were ineffective in adsorbing [(3)H]dihydroalprenolol binding antibodies. We suggest that the likely immunogen was a beta-adrenergic receptor-isoproterenol complex and that immunization with drugs noncovalently bound to their receptors might be a means of raising antibodies to biologically active otherwise nonimmunogenic small molecules. Such antibodies, whose specificity mimics that of a receptor, should also provide useful models for the study of the structure of the receptor binding sites.

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

May 1979

Volume

76

Issue

5

Start / End Page

2263 / 2267

Location

United States

Related Subject Headings

  • Xenopus
  • Species Specificity
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rana pipiens
  • Kinetics
  • Humans
  • Erythrocytes
  • Erythrocyte Membrane
  • Binding Sites, Antibody
 

Citation

APA
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ICMJE
MLA
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Caron, M. G., Srinivasan, Y., Snyderman, R., & Lefkowitz, R. J. (1979). Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands. Proc Natl Acad Sci U S A, 76(5), 2263–2267. https://doi.org/10.1073/pnas.76.5.2263
Caron, M. G., Y. Srinivasan, R. Snyderman, and R. J. Lefkowitz. “Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands.Proc Natl Acad Sci U S A 76, no. 5 (May 1979): 2263–67. https://doi.org/10.1073/pnas.76.5.2263.
Caron MG, Srinivasan Y, Snyderman R, Lefkowitz RJ. Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands. Proc Natl Acad Sci U S A. 1979 May;76(5):2263–7.
Caron, M. G., et al. “Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands.Proc Natl Acad Sci U S A, vol. 76, no. 5, May 1979, pp. 2263–67. Pubmed, doi:10.1073/pnas.76.5.2263.
Caron MG, Srinivasan Y, Snyderman R, Lefkowitz RJ. Antibodies raised against purified beta-adrenergic receptors specifically bind beta-adrenergic ligands. Proc Natl Acad Sci U S A. 1979 May;76(5):2263–2267.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

May 1979

Volume

76

Issue

5

Start / End Page

2263 / 2267

Location

United States

Related Subject Headings

  • Xenopus
  • Species Specificity
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rana pipiens
  • Kinetics
  • Humans
  • Erythrocytes
  • Erythrocyte Membrane
  • Binding Sites, Antibody