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Antipeptide antibodies directed against cytoplasmic rhodopsin sequences recognize the beta-adrenergic receptor.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1987 Mar 25; Vol. 262 (9), pp. 4319-23. - Publication Year :
- 1987
-
Abstract
- Antibodies were made against synthetic peptides that correspond to cytoplasmic domains of rhodopsin, the photopigment protein of the retinal rod. These antipeptide antibodies recognized rhodopsin as detected by immunoblot analysis. Antibodies directed against the cytoplasmic loop between transmembrane domains 1 and 2, as well as those directed against the serine/threonine-rich region of the COOH terminus of bovine rhodopsin, also recognized purified beta-adrenergic receptor isolated from mouse S49 lymphoma cells. In addition, antibodies raised against membrane-associated rhodopsin recognized the beta-adrenergic receptor. Both the antipeptide and anti-rhodopsin antibodies were able to detect a 65-kDa protein band corresponding to the molecular weight of the beta-adrenergic receptor in membranes derived from human placenta, rat adipocytes, and S49 mouse lymphoma cells. Putative recognition sites for the rhodopsin antibodies on the beta-adrenergic receptor are identified, and the significance of the homology between the two proteins is discussed.
- Subjects :
- Adipose Tissue analysis
Amino Acid Sequence
Animals
Cattle
Cytoplasm analysis
Female
Humans
Lymphoma analysis
Mice
Placenta
Pregnancy
Rats
Rod Cell Outer Segment analysis
Antibodies immunology
Peptide Fragments immunology
Receptors, Adrenergic, beta immunology
Retinal Pigments immunology
Rhodopsin immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 262
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 3031071