Glycosylated major urinary protein of the house mouse: characterization of its N-linked oligosaccharides.
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.
Mechref
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Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.
Zidek
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Ma
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Novotny
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MV
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006023:Glycoproteins / Q000032:analysis / Q000737:chemistry; D006031:Glycosylation; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry* / Q000302:isolation & purification; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods
D006023:Glycoproteins; D009844:Oligosaccharides; D011506:Proteins; C035737:major urinary proteins