Structural characterization of N-glycans of cauxin by MALDI-TOF mass spectrometry and nano LC-ESI-mass spectrometry

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Abstract

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 83Asn was a bisecting complex type, Galβ1-4GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1- 2Manα1-6)(GlcNAcβ1-4)-Manβ1-4GlcNAcβ1-4(Fucα1-6) GlcNAc.

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Suzuki, Y., Miyazaki, M., Ito, E., Suzuki, M., Yamashita, T., Taira, H., & Suzuki, A. (2007). Structural characterization of N-glycans of cauxin by MALDI-TOF mass spectrometry and nano LC-ESI-mass spectrometry. Bioscience, Biotechnology and Biochemistry, 71(3), 811–816. https://doi.org/10.1271/bbb.60599

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