@phdthesis{oai:kitami-it.repo.nii.ac.jp:00008434,
 author = {TUMURBAATAR, OYUNJARGAL},
 month = {Sep},
 note = {Lacquer sap is water-in-oil emulsion consisted of urushiols, polysaccharides, glycoproteins, laccase, and stellacyanin that have been used as natural paint in Asian countries. Laccase and stellacyanin are copper?containing glycoproteins, which are heavily glycosylated proteins containing 3 and 15 possible N-glycosylation sites (Asn-x-Thr/Ser), respectively. Structural studies on their carbohydrate structures have not been accomplished yet.
In present study, we isolated laccase and stellacyanin from lacquer acetone powder by continuous ion exchange chromatography using Sephadex CM-50 and DEAE A-50. Protein glycosylarion was characterized using enzymatic digestion, chemical labeling techniques of released N-linked glycan and subsequent mass spectrometric analysis MALDI TOF MS an LC/MS/MS, respectively. We found that three N-glycosylation sites (Asn28, 60 and 102) in lacquer stellacyanin all glycosylated with same complex-type N-linked glycan, constituted with GlcNAc4Man3Gal2Fuc3Xyl1.
Also lacquer laccase glycosylated with complex- and also hybride-type N-linked glycans that are common plant-specific structural units of ?-xylose, core ?-fucose and Lewis epitope (GlcNAc-Gal-Fuc) were observed by MALDI TOF MS. LC/MS/MS analysis of glycopeptides revealed that 13 N-glycosylation sites in laccase were glycosylated frequently with complex type N-glycan, GlcNAc4Man3Gal2Fuc3Xyl1, and among them Asn5, 233 and 381 were also found to be glycosylated with hybride?type N-glycan, mainly GlcNAc2-3Man4-5Fuc1Xyl1. Glycopeptides which carry possible N-glycosylation sites at Asn 364 and 519 were not confirmed by LC/MS/MS analysis.},
 school = {北見工業大学},
 title = {Enzymatic Digestion and Mass Spectroscopies of N-Linked Glycans in Lacquer Stellacyanin and Laccase from Rhus vernicifera},
 year = {2015}
}