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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structural Characterization of N-Glycans of Cauxin by MALDI-TOF Mass Spectrometry and Nano LC-ESI-Mass Spectrometry.

Cauxin is a carboxylesterase-like glycoprotein excreted as a major component of cat urine. Cauxin contains four putative N-glycosylation sites. We characterized the structure of an N-linked oligosaccharide of cauxin using nano liquid chromatography (LC)-electrospray ionization ( ESI) and matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight mass spectrometry (MALDI-QIT-TOF MS) and MS/MS, and high-performance liquid chromatography (HPLC) with an octadecylsilica (ODS) column. The structure of the N-linked oligosaccharide of cauxin attached to (83)Asn was a bisecting complex type, Galbeta1-4GlcNAcbeta1-2Manalpha1-3(Galbeta1-4GlcNAcbeta1-2Manalpha1-6)(GlcNAcbeta1-4)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAc.[1]

References

  1. Structural Characterization of N-Glycans of Cauxin by MALDI-TOF Mass Spectrometry and Nano LC-ESI-Mass Spectrometry. Suzuki, Y., Miyazaki, M., Ito, E., Suzuki, M., Yamashita, T., Taira, H., Suzuki, A. Biosci. Biotechnol. Biochem. (2007) [Pubmed]
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