Membrane receptors of human erythrocytes for bacterial lipopolysaccharide (LPS).
The binding specificity of bacterial lipopolysaccharide (LPS) was investigated by inhibition experiments of the binding of 3H-labelled Escherichia coli lipopolysaccharide (LPS) AND 3H-labelled Salmonella minnesota R595 glycolipid and lipid A to human erythrocytes using various glycoproteins as inhibitors. PAS-1 glycoprotein and band-3 glycoprotein of human erythrocyte membranes exerted strong inhibitory activity. To characterize membrane receptors for LPS, solubilized membranes of human erythrocytes were subjected to affinity chromatography with an affinity adsorbent prepared by coupling S. minnesota R595 glycolipid to activated Sepharose 4B. Band-3 and PAS-1 glycoproteins were identified as major receptor sites.
D001665:Binding Sites; D002846:Chromatography, Affinity; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D004926:Escherichia coli; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism*; D012475:Salmonella; D012795:Sialoglycoproteins / Q000378:metabolism
D008070:Lipopolysaccharides; D012795:Sialoglycoproteins