Simultaneous analysis of glycosaminoglycan-protein linkage regiona and glycosylation site of proteoglycan
| Project/Area Number |
24550089
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Analytical chemistry
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| Research Institution | Hokkaido University |
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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)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
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| 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 / 分析化学 / ピラゾロン / マイクロ波 / O結合型糖鎖 |
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| 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.
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Report
(4 results)
Research Products
(18 results)
