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Glycoprotein Properties of the Solubilized Atrial Muscarinic Acetylcholine Receptor
Author(s) -
Herron G. Scott,
Schimerlik Michael I.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb00840.x
Subject(s) - muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m2 , acetylcholine , muscarinic acetylcholine receptor m5 , muscarinic acetylcholine receptor m3 , muscarinic acetylcholine receptor m4 , solubilization , acetylcholine receptor , chemistry , receptor , muscarinic acetylcholine receptor m1 , pharmacology , neuroscience , biochemistry , medicine , biology
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 β(1 → 4)‐linked oligomers.