Title : A comparative study of the N-linked oligosaccharide structures of human
IgG subclass
proteins
Abstract :
- Quantitative oligosaccharide profiles were determined for each of 18 human IgG paraproteins representing the four subclasses
- Each para protein exhibits a unique profile that may be substantially different from that observed for polyclonal IgG
- The IgG2 and some IgG3 proteins analysed exhibit a predominance of oligosaccharide moieties having galactose on the Man(alpha 1----3) arm rather than the Man(alpha 1----6) arm; it was previously held that galactosylation of the Man(alpha 1----6) arm is preferred, as observed for IgG1 , IgG4 and polyclonal IgG
- An IgG4 protein is reported that has galactosylated Man(alpha 1----3) and Man(alpha 1----6) arms on both Fc-localized carbohydrate moieties; previous findings suggested that such fully glycosylated structures could not be accommodated within the internal space of the C gamma 2 domains
- Unusual monoantennary oligosaccharides present in IgG2 and IgG3 proteins were isolated and their structures determined
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. proteins, , proteins, the N-linked oligosaccharide structures, -
- 3. galactose, , -, the Man(alpha 1----3) arm, -
- 3. galactose, , -, the Man(alpha 1----6) arm, -
- 5. present, , IgG2, Unusual monoantennary oligosaccharides, -
- 5. present, , IgG3 proteins, Unusual monoantennary oligosaccharides, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):