Isolation of glycopeptides from the lectin-stimulated human peripheral lymphocyte cell surface.
Three radioactive glycopeptides were isolated from human peripheral lymphocytes stimulated with Wistaria floribunda mitogen in the presence of D-[14C]glucosamine hydrochloride by mild trypsin digestion followed by gel filtration and preparative high-voltage paper electrophoresis. The carbohydrate compositions of these glycopeptides suggest that one has a sugar chain of the type found in serum glycoproteins, consisting of sialic acid, galactose, N-acetylglucosamine, mannose, and fucose in a molar ratio of 2:2:4:2:1, and the other two have sugar chains like those of mucins, consisting of sialic acid, galactose, and N-acetylgalactosamine in a molar ratio of 1 or 2:1:1. The results of enzymic degradation with purified glycosidases indicate that these sugar chains are similar in structure to their counterparts in human erythrocyte membranes.
D002241:Carbohydrates / Q000032:analysis; D002462:Cell Membrane / Q000378:metabolism; D006020:Glycopeptides / Q000302:isolation & purification / Q000378:metabolism; D006026:Glycoside Hydrolases; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis
D002241:Carbohydrates; D006020:Glycopeptides; D037102:Lectins; D008565:Membrane Proteins; D010446:Peptide Fragments; D006026:Glycoside Hydrolases