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The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling.

Publication ,  Journal Article
Shorr, RG; Strohsacker, MW; Lavin, TN; Lefkowitz, RJ; Caron, MG
Published in: J Biol Chem
October 25, 1982

The beta 1-adrenergic receptor of turkey erythrocytes has been purified by a combination of affinity and high performance steric exclusion chromatography. These procedures provide preparations with specific activities of greater than 15,000 pmol/mg of protein with an overall recovery of approximately 30% of the receptor activity solubilized from membrane preparations. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of radioiodinated purified receptor reveals two bands of labeled protein with apparent Mr = 40,000 +/- 2,000 and 45,000 +/- 3,000 in a 3-4:1 ratio. These same two peptides can also be labeled specifically and in approximately the same ration in both membranes and purified preparations using the photoaffinity probe 125I-labeled p-azidobenzylcarazolol. When the two purified polypeptides are completely separated by high performance liquid chromatography and subjected to detailed ligand binding studies, identical beta 1-adrenergic specificities are found for the two receptor forms. Preliminary characterization of these two proteins by partial protease digestion suggests a large degree of similarity between them, albeit with some significant differences. These results demonstrate that both purification and photoaffinity labeling identify two polypeptides in turkey erythrocyte membranes as containing a beta 1-adrenergic receptor binding site. The functional and structural relationships of these two forms of the receptor remain to be elucidated.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

October 25, 1982

Volume

257

Issue

20

Start / End Page

12341 / 12350

Location

United States

Related Subject Headings

  • Turkeys
  • Trypsin
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Photochemistry
  • Papain
  • Molecular Weight
  • Isoelectric Focusing
  • Erythrocytes
  • Chymotrypsin
 

Citation

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Shorr, R. G., Strohsacker, M. W., Lavin, T. N., Lefkowitz, R. J., & Caron, M. G. (1982). The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling. J Biol Chem, 257(20), 12341–12350.
Shorr, R. G., M. W. Strohsacker, T. N. Lavin, R. J. Lefkowitz, and M. G. Caron. “The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling.J Biol Chem 257, no. 20 (October 25, 1982): 12341–50.
Shorr RG, Strohsacker MW, Lavin TN, Lefkowitz RJ, Caron MG. The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling. J Biol Chem. 1982 Oct 25;257(20):12341–50.
Shorr RG, Strohsacker MW, Lavin TN, Lefkowitz RJ, Caron MG. The beta 1-adrenergic receptor of the turkey erythrocyte. Molecular heterogeneity revealed by purification and photoaffinity labeling. J Biol Chem. 1982 Oct 25;257(20):12341–12350.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

October 25, 1982

Volume

257

Issue

20

Start / End Page

12341 / 12350

Location

United States

Related Subject Headings

  • Turkeys
  • Trypsin
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Photochemistry
  • Papain
  • Molecular Weight
  • Isoelectric Focusing
  • Erythrocytes
  • Chymotrypsin