Proteolysis-associated deglycosylation of beta 1-adrenergic receptor in turkey erythrocytes and membranes.
A protease that can be inhibited by glutathione, dithiothreitol, and o-phenanthroline but not by ethylenediaminetetraacetic acid converts the 50-kilodalton beta-adrenergic receptor in turkey erythrocyte membranes to a 40-kDa polypeptide which retains the specific ligand binding site. This conversion is attenuated in intact erythrocytes. The large 50-kDa peptide contains N-linked, complex carbohydrates and is retained on wheat germ agglutinin-Sepharose. The 40-kDa product of proteolysis does not bind to the wheat germ agglutinin and can thus be separated from the 50-kDa polypeptide by lectin chromatography. However, the large difference in molecular weights of the two receptor peptides cannot be accounted for solely by the different extent of glycosylation.
Jürss
R
R
Hekman
M
M
Helmreich
E J
EJ
D000818:Animals; D002846:Chromatography, Affinity; D004082:Dihydroalprenolol / Q000097:blood; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000097:blood*; D011943:Receptors, Adrenergic, beta / Q000302:isolation & purification / Q000378:metabolism*; D014422:Turkeys
D006023:Glycoproteins; D011943:Receptors, Adrenergic, beta; D004082:Dihydroalprenolol; D010447:Peptide Hydrolases