Simultaneous analysis of glycosaminoglycan-protein linkage regiona and glycosylation site of proteoglycan

2014 Fiscal Year Final Research Report

• Project/Area Number: 24550089
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Analytical chemistry
• Research Institution: Hokkaido University
• Principal Investigator: FURUKAWA Jun-ichi 北海道大学, 先端生命科学研究科(研究院), 特任助教 (30374193)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: プロテオグリカン / グライコミクス / β脱離反応 / グリコサミノグリカン

Outline of Final Research Achievements

Serine (Ser) and threonine (Thr) residues can be modified by various types of sugar chains, such as the O-GalNAc type typical of mucin and the O-GlcNAc, O-Fuc, O-Man, and O-Xyl types. The characterization of O-glycans has remained particularly challenging because no analogous endoglycosidase is known, and alternative chemical protocols are either incomplete, lack specificity, or degrade products. We recently reported a novel method for the analysis of Ser/Thr post-translational modifications, in which samples were subjected to β-elimination in the presence of pyrazolone derivatives. We report here applications of BEP reaction for the analyses of glycosaminoglycan-protein linkage regiona, GAG disaccharides, and glycosylation site of proteoglycan.

Free Research Field

分析化学