Abstract
This paper describes the structures of the asparagine-linked oligosaccharides of two forms of guinea-pig Factor B of the alternative complement pathway with different M(r) values. Oligosaccharides were quantitatively liberated from both glycoproteins by hydrazinolysis, fractionated by paper electrophoresis and Bio-Gel P-4 column chromatography, and their structures determined by sequential exoglycosidase digestions in conjunction with methylation analysis. Both glycoproteins were shown to have the same biantennary complex-type oligosaccharides but it is suggested that they contain different numbers of oligosaccharide chains.
| Original language | English |
|---|---|
| Pages (from-to) | 533-535 |
| Number of pages | 3 |
| Journal | Biochemical Journal |
| Volume | 272 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1990 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology