Glycoprotein properties of the solubilized atrial muscarinic acetylcholine receptor.
The muscarinic acetylcholine receptor from porcine atria exhibits sialoglycoprotein characteristics based on its sensitivity to neuraminidase digestion and its ability to interact specifically with lectin affinity resins when solubilized with a digitonin/cholate mixed detergent system. Differential lectin binding properties of the neuraminidase-treated and untreated receptor suggest that high-affinity binding to immobilized wheat germ agglutinin is accomplished through the presence of both terminal sialic acid and internal N-acetylglucosamine or its beta(1 leads to 4)-linked oligomers.
D000818:Animals; D006023:Glycoproteins / Q000032:analysis*; D006325:Heart Atria / Q000032:analysis; D037102:Lectins / Q000378:metabolism; D009206:Myocardium / Q000032:analysis*; D009439:Neuraminidase / Q000378:metabolism; D011813:Quinuclidinyl Benzilate / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000032:analysis*; D012995:Solubility; D013552:Swine; D014909:Wheat Germ Agglutinins
D006023:Glycoproteins; D037102:Lectins; D011950:Receptors, Cholinergic; D014909:Wheat Germ Agglutinins; D011813:Quinuclidinyl Benzilate; D009439:Neuraminidase