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  • Title: Primary structure of two sialylated triantennary glycans from human serotransferrin.
    Author: Spik G, Debruyne V, Montreuil J, van Halbeek H, Vliegenthart JF.
    Journal: FEBS Lett; 1985 Apr 08; 183(1):65-9. PubMed ID: 3979568.
    Abstract:
    Glycopeptides obtained from human serotransferrin by pronase digestion were separated into two fractions by affinity chromatography on Con A-Sepharose. The retarded fraction (85% of total glycopeptides) contained sialylated biantennary glycans of the N-acetyllactosaminic type, the primary structure of which has been previously determined. The non-retained fraction (15% of total glycopeptides) consisted of two isomeric triantennary glycans of the N-acetyllactosaminic type. The primary structure have been elucidated by methylation analysis and 500 MHz 1H-NMR spectroscopy. Both contain an additional NeuAc(alpha 2----3)Gal(beta 1----4)GlcNAc antenna. The latter is linked to C-4 of the (alpha 1----3) bound Man residue in 45% of the glycans in the non-retained fraction but to C-6 of the (alpha 1----6) bound Man residue, in the remaining 55% of the glycans in this fraction.
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