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Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity.

Publication ,  Journal Article
Sibley, DR; Peters, JR; Nambi, P; Caron, MG; Lefkowitz, RJ
Published in: Biochem Biophys Res Commun
March 15, 1984

The potent photoaffinity probe [125I]p-azidobenzylcarazolol was used to identify beta-adrenergic receptors from turkey erythrocytes. Two peptides were specifically labeled with apparent Mr = 39,000 and 49,000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The ratio of labeling of these peptides was found to be dependent on the method of tissue preparation. Thus, the Mr = 39,000/Mr = 49,000 ratio was 1:2 when labeling was done on intact cells, 1:1 for labeling of crude membranes, and 4:1 for purified membrane preparations. Moreover, incubation of intact cells or either membrane preparation at 37 degrees C led to a diminution of the Mr = 49,000 labeled peptide which was associated with a stoichiometric increase in the Mr = 39,000 form of the receptor. These results suggest that the turkey erythrocyte beta-adrenergic receptor is a protein of Mr = 49,000 and that the commonly observed Mr = 39,000 peptide is derived from this protein.

Duke Scholars

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

March 15, 1984

Volume

119

Issue

2

Start / End Page

458 / 464

Location

United States

Related Subject Headings

  • Turkeys
  • Receptors, Adrenergic, beta
  • Propanolamines
  • Photochemistry
  • Molecular Weight
  • Erythrocyte Membrane
  • Carbazoles
  • Biochemistry & Molecular Biology
  • Azides
  • Animals
 

Citation

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Sibley, D. R., Peters, J. R., Nambi, P., Caron, M. G., & Lefkowitz, R. J. (1984). Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity. Biochem Biophys Res Commun, 119(2), 458–464. https://doi.org/10.1016/s0006-291x(84)80271-5
Sibley, D. R., J. R. Peters, P. Nambi, M. G. Caron, and R. J. Lefkowitz. “Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity.Biochem Biophys Res Commun 119, no. 2 (March 15, 1984): 458–64. https://doi.org/10.1016/s0006-291x(84)80271-5.
Sibley DR, Peters JR, Nambi P, Caron MG, Lefkowitz RJ. Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity. Biochem Biophys Res Commun. 1984 Mar 15;119(2):458–64.
Sibley, D. R., et al. “Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity.Biochem Biophys Res Commun, vol. 119, no. 2, Mar. 1984, pp. 458–64. Pubmed, doi:10.1016/s0006-291x(84)80271-5.
Sibley DR, Peters JR, Nambi P, Caron MG, Lefkowitz RJ. Photoaffinity labeling of turkey erythrocyte beta-adrenergic receptors: degradation of the Mr = 49,000 protein explains apparent heterogeneity. Biochem Biophys Res Commun. 1984 Mar 15;119(2):458–464.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

March 15, 1984

Volume

119

Issue

2

Start / End Page

458 / 464

Location

United States

Related Subject Headings

  • Turkeys
  • Receptors, Adrenergic, beta
  • Propanolamines
  • Photochemistry
  • Molecular Weight
  • Erythrocyte Membrane
  • Carbazoles
  • Biochemistry & Molecular Biology
  • Azides
  • Animals