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International Journal of Polymer Science
Volume 2015, Article ID 547907, 9 pages
Research Article

Enzymatic Digestion and Mass Spectroscopies of N-Linked Glycans in Lacquer Stellacyanin from Rhus vernicifera

1Department of Biological and Environmental Chemistry, Kitami Institute of Technology, 165 Koen-cho, Kitami, Hokkaido 090-8507, Japan
2Research Center for Environmentally Friendly Materials Engineering, Muroran Institute of Technology, 27-1 Mizumoto-cho, Muroran, Hokkaido 050-8585, Japan

Received 5 January 2015; Accepted 15 February 2015

Academic Editor: Yulin Deng

Copyright © 2015 Oyunjargal Tumurbaatar and Takashi Yoshida. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Lacquer stellacyanin was isolated and purified from lacquer acetone powder by continuous Sephadex column chromatographies using Sephadex C-50, DEAE A-50, and C-50 gels. The purified lacquer stellacyanin had a blue color with one major and three minor bands around 26 k Dain SDS PAGE. Trypsin- and chymotrypsin-treated lacquer stellacyanins were examined by LC/MS/MS to determine three N-glycosylation sites (N28, N60, and N102) and were further analyzed by MALDI TOF MS, indicating that the N-linked glycans were attached to the three asparagine (Asn) sites, respectively. In addition, after trypsin digestion and PNGase A and PNGase F treatments to cleave N-linked glycans from the Asn sites, it was found that lacquer stellacyanin had a xylose containing a biantennary N-linked glycan with core fucosylation consisting of 13 sugar residues (a complex type N-linked glycan) by MALDI TOF MS analysis. This is the first report on the structure of an N-linked glycan in lacquer stellacyanin.