Abstract
A minor component of the major urinary protein complex of the house mouse was chromatographically isolated and ascertained to be a previously suspected glycoprotein. Using highly sensitive mass-spectrometric techniques for sequencing and linkage analysis, the N-linked oligosaccharides of this glycoprotein were characterized. They were determined to be of the complex type with a wide heterogeneity. The heterogeneity was due to both the degree of sialylation and the presence of galactose residues in either β(1-3) or β(1-4) linkages. The biantennary structures were the most pronounced glycans, while tri- and tetraantennary entities were minor.
Original language | English |
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Pages (from-to) | 231-235 |
Number of pages | 5 |
Journal | Glycobiology |
Volume | 10 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2000 |
Keywords
- House mouse
- Mass spectrometry
- Oligosaccharide sequencing
- Pheromone-binding protein