Structural Studies of the Sugar Chains of Cold-Insoluble Globulin Isolated from Human Plasma1

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Abstract
The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis. These oligosaccharides were N-acetylated and could be labeled by reduction with NaB[3]4 The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine linked sugar chains in one molecule. More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2. By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Galβ1→4GlcNAcβ1→2Manα1→6(NeuAcα2→6Galβ1→4GlcNAcβ1→2Manαl→3) Manβ1→4GlcNAcβ1 →4GlcNAc and NeuAcα2→6Galβ→4GlcNAcβ1→6 (NeuAcα2→6Galβ→4GlcNAcβ→2Manα→3)-Manβ41→4GlcNAcβ→4GlcNAc.

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