Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Effect of removal of the glycosylation site from the beta-adrenergic receptor

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6374189
The beta-adrenergic receptor (BAR) has been modified by oligonucleotide-directed mutagenesis to remove two possible N-linked glycosylation sites near the amino terminus of the protein, and the mutant protein expressed in mammalian cells. The expressed protein has an apparent molecular weight of 47,000 daltons, the expected size of the non-glycosylated receptor, as assessed by protein immunoblotting with an antibody directed against a synthetic peptide corresponding to a region of the BAR. This mutant BAR showed an attenuated level of /sup 125/I-cyanopindolol binding activity, representing a decreased amount of active BAR than was detected by immunoblotting and suggesting the presence of inactive receptor protein. However, the affinity of the non-glycosylated receptor for agonists and antagonists was normal, suggesting that the lack of glycosylation may affect the turnover rate of active receptors, without altering its intrinsic binding properties.
Research Organization:
Merck Sharp and Dohm Research Labs., West Point, PA
OSTI ID:
6374189
Report Number(s):
CONF-870644-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 46:6
Country of Publication:
United States
Language:
English