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学科主题: 分析化学
题名: Integration of click maltose hydrophilic interaction chromatography, SCX preolumn and PNGase F immobilized enzymatic reactor for N-linked glycosylation sites profiling
作者: Qu YY(曲焱焱) ;  Yuan HM(袁辉明) ;  Zhang LH(张丽华) ;  Liang Z(梁振) ;  Zhang YK(张玉奎)
会议文集: 26th International Symposium on Microscale Bioseparations
会议名称: 26th International Symposium on Microscale Bioseparations
会议日期: 2011-5-1
出版日期: 2011
会议地点: 圣地亚哥
通讯作者: 张丽华
出版者: 待补充
出版地: 待补充
合作性质: 墙报
部门归属: 1810
主办者: CASSS
摘要: N-glycosylation is one of the most common and complex post-translational modifications of proteins, and plays an important role in many cellular interactions and pathogenesis of diseases. Global mapping of N-linked glycosylation sites is a prerequisite for fully understanding the biological functions of N-linked glycoproteins. Therefore, the development of a fast and specific strategy to achieve high-throughput and high-sensitivity glycoproteome analysis becomes imperative. The traditional N-linked glycosylation sites profiling is usually off-line performed, with drawbacks such as long analysis time, resultant sample loss and manual manipulation. In our recent work, an integrated sample pretreatment system, composed of a click maltose hydrophilic interaction chromatography (HILIC) column, a strong cation exchange (SCX) precolumn and a PNGase F immobilized enzymatic reactor (IMER), was established for the simultaneous glycopeptide enrichment, sample buffer exchange, and on-line deglycosylation. Compared with the conventional off-line method, the analysis time, including glycopeptide enrichment and deglycosylation was shortened to 1 h, and the detection limit as low as 5 fmol was achieved. Moreover, such a system was successfully applied for analyzing the digest of soluble fraction extracted from rat brain. A total of 120 unique glycoprotein groups and 196 N-linked glycosylation sites were identified, with the injected digests amount as 6 µg. All these results demonstrated that the integrated system is of great promise to achieve fast and high sensitive N-linked glycosylation sites profiling, which could be further online coupled with nano HPLC-ESI/MS/MS to achieve high-throughput glycoproteome analysis.
英文摘要: N-glycosylation is one of the most common and complex post-translational modifications of proteins, and plays an important role in many cellular interactions and pathogenesis of diseases. Global mapping of N-linked glycosylation sites is a prerequisite for fully understanding the biological functions of N-linked glycoproteins. Therefore, the development of a fast and specific strategy to achieve high-throughput and high-sensitivity glycoproteome analysis becomes imperative. The traditional N-linked glycosylation sites profiling is usually off-line performed, with drawbacks such as long analysis time, resultant sample loss and manual manipulation. In our recent work, an integrated sample pretreatment system, composed of a click maltose hydrophilic interaction chromatography (HILIC) column, a strong cation exchange (SCX) precolumn and a PNGase F immobilized enzymatic reactor (IMER), was established for the simultaneous glycopeptide enrichment, sample buffer exchange, and on-line deglycosylation. Compared with the conventional off-line method, the analysis time, including glycopeptide enrichment and deglycosylation was shortened to 1 h, and the detection limit as low as 5 fmol was achieved. Moreover, such a system was successfully applied for analyzing the digest of soluble fraction extracted from rat brain. A total of 120 unique glycoprotein groups and 196 N-linked glycosylation sites were identified, with the injected digests amount as 6 µg. All these results demonstrated that the integrated system is of great promise to achieve fast and high sensitive N-linked glycosylation sites profiling, which could be further online coupled with nano HPLC-ESI/MS/MS to achieve high-throughput glycoproteome analysis.
语种: 英语
内容类型: 会议论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/116025
Appears in Collections:中国科学院大连化学物理研究所_会议论文

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Recommended Citation:
Qu YY,Yuan HM,Zhang LH,et al. Integration of click maltose hydrophilic interaction chromatography, SCX preolumn and PNGase F immobilized enzymatic reactor for N-linked glycosylation sites profiling[C]. 见:26th International Symposium on Microscale Bioseparations. 圣地亚哥. 2011-5-1.
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