Occurrence of the Y determinant on the N-glycosidic carbohydrate units of human gamma-seminoprotein.
500-MHz H-NMR spectroscopy of the oligosaccharides derived from gamma-seminoprotein, a human seminal plasma glycoprotein, revealed considerable microheterogeneity both with respect to the degree of branching and with regard to the peripheral sugars. Although the protein possesses only one N-glycosylation site, di-, tri- and tetra-antennary glycans in a ratio of 40:15:45 were found to be present. Moreover, certain branches of the tri- and tetra-antennas contain one or two Fuc residues which form part of the SSEA-1 and Y determinants. It should be noted that this is the first report that describes the occurrence and localization of the Y determinant, i.e. Fuc alpha (1----2)Gal beta (1----4) [Fuc alpha (1----3)]GlcNAc beta (1----.), in an N-glycan of a glycoprotein.
D002236:Carbohydrate Conformation; D003208:Concanavalin A; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D009844:Oligosaccharides / Q000032:analysis*; D011134:Polysaccharides; D029584:Prostatic Secretory Proteins; D011506:Proteins / Q000032:analysis*; D029589:Seminal Plasma Proteins
D009844:Oligosaccharides; D011134:Polysaccharides; D029584:Prostatic Secretory Proteins; D011506:Proteins; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein; D003208:Concanavalin A