title: Structural study of the asparagine-linked oligosaccharides of lipophorin in locusts.
abstract: The complete structure of oligosaccharides from locust lipophorin was studied. The asparagine-linked oligosaccharides were first liberated from the protein moiety of lipophorin by digestion with almond glycopeptidase (N-oligosaccharide glycopeptidase, EC 3.5.1.52). Two major oligosaccharides (E and F), separated by subsequent thin-layer chromatography, were analyzed by methylation analysis and 1H-NMR. Based on the experimental data, the whole structure of oligosaccharide E was identified as Man alpha 1----2Man alpha 1----6(Man alpha 1----2Man alpha 1----3) Man alpha 1----6(Man alpha 1----2Man alpha 1----2Man alpha 1----3)Man beta 1----4GlcNAc beta 1----4GlcNAc. The data also revealed that oligosaccharide F is identical with oligosaccharide E in the structure, except for one glucose residue that is linked to the nonreducing terminal Man alpha 1----2 residue.
mesh_terms: D000818:Animals; D001216:Asparagine / Q000302:isolation & purification*; D002240:Carbohydrate Sequence; D002352:Carrier Proteins / Q000302:isolation & purification*; D006110:Grasshoppers / Q000378:metabolism*; D008074:Lipoproteins; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D009844:Oligosaccharides / Q000302:isolation & purification*
chemical_list: D002352:Carrier Proteins; D008074:Lipoproteins; D009844:Oligosaccharides; C032830:lipophorin; D001216:Asparagine