详细信息
Selective enrichment of N-linked glycopeptides and glycans by using a dextran-modified hydrophilic material ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:Selective enrichment of N-linked glycopeptides and glycans by using a dextran-modified hydrophilic material
作者:Chen, Linlin[1,2];Ding, Di[2];Sheng, Qianying[3];Yu, Long[4];Liu, Xiuping[1,2];Liang, Xinmiao[4]
机构:[1]Fudan Univ, Peoples Hosp 5, Shanghai, Peoples R China;[2]Fudan Univ, Sch Basic Med Sci, Dept Pathol, Shanghai, Peoples R China;[3]East China Univ Sci & Technol, Shanghai Key Lab Funct Mat Chem, Shanghai, Peoples R China;[4]Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
年份:2018
卷号:41
期号:9
起止页码:2003
外文期刊名:JOURNAL OF SEPARATION SCIENCE
收录:;EI(收录号:20180704787256);WOS:【SCI-EXPANDED(收录号:WOS:000434139000012)】;
基金:This work was supported by grants from the National Natural Science Foundation of China (81470857 to X.P.L), the Natural Science Foundation of Shanghai (16ZR1407600), and Shanghai Sailing Program (16YF1402400).
语种:英文
外文关键词:dextran-bonded silica; glycans; glycopeptides; hydrophilic interaction liquid chromatography; Sepharose
摘要:Glycosylation analysis of proteins from biological sources utilizing mass spectrometry based approaches is challenging due to the relatively low abundance of glycopeptides, the structural diversity of glycans, and the coexisting matrices. In this study, a customized dextran-bonded silica-based stationary phase was introduced for selective enrichment of glycopeptides and glycans from complex biological samples. This material has exhibited superior selectivity and broader glycosylation site coverage over commercial Sepharose in glycoproteomic evaluation. Additionally, the glycomic analysis of fetuin, alpha(1)-acid glycoprotein, and human serum N-glycome also indicated the relatively higher sensitivity, selectivity, and glycoform coverage of dextran-bonded silica than that of Sepharose and porous graphitized carbon. Therefore, the dextran-bonded silica is expected to make contributions in the fields of glycoproteomics and glycomics.
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