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.
Suzuki
Yusuke
Y
Sphingolipid Expression Laboratory, Supra-Biomolecular System Research Group, RIKEN Frontier Research System, Wako, Saitama, Japan.
Miyazaki
Masao
M
Ito
Emi
E
Suzuki
Minoru
M
Yamashita
Tetsuro
T
Taira
Hideharu
H
Suzuki
Akemi
A
D000595:Amino Acid Sequence; D000818:Animals; D043182:Carboxylesterase / Q000737:chemistry*; D002415:Cats; D006031:Glycosylation; D008969:Molecular Sequence Data; D036103:Nanotechnology; D011134:Polysaccharides / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D011134:Polysaccharides; D043182:Carboxylesterase; C515680:cauxin protein, Felis catus