The structure of unit-B-type glycopeptides from porcine thyroglobulin

Abstract

The structure of Unit B-type glycopeptides (monosialo-type and disialo-type) was investigated by Smith degradation, methylation, and mass spectral analysis. These glycopeptides contain three peripheral sugar chains. Two are composed of d-galactose residues linked at C-6 and 2-acetamido-2-deoxy- d-glucose residues linked at C-4, and the other is composed of a dD-galactose residue linked at C-6, a 2-acetamido-2-deoxy- d-glucose residue linked at C-4, and a d-mannose residue linked at C-2. Most of these peripheral sugar chains are linked to two inner d-mannose residues which are substituted at C-3 and C-6, and constitute branching points. l-Fucose and N-acetyl-neuraminic acid residues are nonreducing terminal groups, and a di- N-acetylchito-biose moiety is linked to an asparagine residue in the peptide moiety. By methylation analysis of the oligosaccharide obtained by hydrazinolysis of the disialoglycopeptide, the l-fucose residue was found to be linked to C-6 of the 2-acetamido-2-deoxy- d-glucose residue linked to the asparagine residue. From these results, and from the previously reported data on the sugar sequence and the anomeric configurations of the linkages between sugar residues, structures for these glycopeptides are proposed.