Structures of the carbohydrate moiety attached to one site in the first domain of turkey ovomucoid: elucidation by 1H-n.m.r. spectroscopy.
1H-N.m.r. spectroscopy was used to elucidate the primary structures of the carbohydrate moiety attached to asparagine at residue 53 in the first domain of turkey ovomucoid, a serine proteinase inhibitor. The carbohydrate moiety is a heterogeneous mixture of three structurally closely related complex-type oligosaccharides. Of the total carbohydrate moiety, 61% is tetra-antennary with terminal galactose and with an intersecting N-acetylglucosamine, and containing an additional N-acetylglucosamine (10') attached to mannose (4'). Another 23% is tri-antennary with terminal galactose and with an intersecting N-acetylglucosamine. The remaining 16% is tri-antennary with terminal galactose (6 and 8 only), with an intersecting N-acetylglucosamine.
J M
JM
Risley
R L
RL
Van Etten
D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D004527:Egg Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009844:Oligosaccharides / Q000032:analysis*; D010059:Ovomucin; D014422:Turkeys
D004527:Egg Proteins; D009844:Oligosaccharides; D010059:Ovomucin; D001216:Asparagine