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.
No takes yet. Share an insight, caveat, or question.
Herron et al. (1983) studied this question.
Synapse has enriched 2 closely related papers on similar clinical questions. Consider them for comparative context: