Enzymatic Digestion and Mass Spectroscopies of N-Linked Glycans in Lacquer Stellacyanin from Rhus vernicifera. (30th August 2015)

• Record Type: Journal Article
• Authors: Tumurbaatar, Oyunjargal; Yoshida, Takashi
• Other Names: Deng Yulin Academic Editor.
• Is Part Of: International journal of polymer science. Volume 2015(2015)
• Publication Date: 2015-08-30
• Subjects: Polymers -- Periodicals; Polymers; Periodicals; 547.7
• DOI: 10.1155/2015/547907
• Languages: English
• ISSNs: 1687-9422

Abstract

Abstract : 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.