Structural study of N-linked sugar chains of sheep erythrocyte membrane glycoproteins.
Our previous study showed that non-reducing terminal galactose residues of N-linked sugar chains present in sheep erythrocyte membrane glycoproteins are important for rosette formation with T lymphoblastic cells [Ogasawara et al. (1995) Immunol Lett 48: 35-38]. As a first step to elucidate the significant structures of sugar chains involved in rosette formation, we analysed N-linked sugar chains released from the membrane glycoproteins by hydrazinolysis. The oligosaccharides were labeled with NaB3H4 and fractionated using columns of Aleuria aurantia lectin-Sepharose, MonoQ and Bio-Gel P-4. Structural analyses of oligosaccharides by sequential exoglycosidase digestion in combination with methylation analysis revealed that the membrane glycoproteins contain bi- (19%), tri- (33%), and tetraantennary (44%) complex-type oligosaccharides and that the oligosaccharides having exposed galactose residues amount to 40% of the total.
Kusui
K
K
Department of Biochemistry, Institute of Medical Science, University of Tokyo, Japan.
Takasaki
S
S
D000818:Animals; D002240:Carbohydrate Sequence; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008745:Methylation; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry; D012397:Rosette Formation; D012756:Sheep; D012795:Sialoglycoproteins / Q000737:chemistry; D013601:T-Lymphocytes / Q000166:cytology
D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D012795:Sialoglycoproteins