Journal
GLYCOBIOLOGY
Volume 10, Issue 3, Pages 231-235Publisher
OXFORD UNIV PRESS
DOI: 10.1093/glycob/10.3.231
Keywords
house mouse; mass spectrometry; oligosaccharide sequencing; pheromone-binding protein
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM024349] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS [R01DC002418] Funding Source: NIH RePORTER
- NIDCD NIH HHS [DC02418] Funding Source: Medline
- NIGMS NIH HHS [GM24349] Funding Source: Medline
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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 beta(1-3) or beta(1-4) linkages. The biantennary structures were the most pronounced glycans, while tri- and tetraantennary entities were minor.
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