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Glycobiology, 2000, Vol. 10, No. 3 231-235
© 2000 Oxford University Press

Glycosylated major urinary protein of the house mouse: characterization of its N-linked oligosaccharides

Yehia Mechref1, Lukas Zidek, Weidong Ma and Milos V. Novotny2

Department of Chemistry, Indiana University, Bloomington, IN 47405, USA

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 ß(1–3) or ß(1–4) linkages. The biantennary structures were the most pronounced glycans, while tri- and tetraantennary entities were minor.

1 Present address: Department of Chemistry, Faculty of Science, United Arab Emirates University, P.O. Box 17551, Al-Ain, UAE

2 To whom correspondence should be addressed


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