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N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry |
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| Authors: | SONG LiNa WANG JingLan LIU JinFeng LU Zhuang SUI ShaoHui JIA Wei YANG Bing CHI Hao WANG LeHeng HE SiMin YU WenFeng MENG LingYan CHEN Shuo PENG Xu LIANG YiMin CAI Yun & QIAN XiaoHong State Key Laboratory of Proteomics Beijing Proteome Research Center Beijing Institute of Radiation Medicine Beijing China |
| Affiliation: | SONG LiNa1,WANG JingLan1,LIU JinFeng1,LU Zhuang1,3,SUI ShaoHui1,JIA Wei1,YANG Bing1,CHI Hao2,WANG LeHeng2,HE SiMin2,YU WenFeng1,MENG LingYan1,CHEN Shuo1,PENG Xu1,LIANG YiMin1,CAI Yun1 & QIAN XiaoHong1 1State Key Laboratory of Proteomics,Beijing Proteome Research Center,Beijing Institute of Radiation Medicine,Beijing 102206,China,2Institute of Computing Technology,Chinese Academy of Sciences,Beijing 100190,3Beijing Institute of Biotechnology,Beijing 100081 |
| Abstract: | Glycosylation is the most versatile and one of the most significant protein post-translational modifications. It is generally classified into three categories according to the amino acid to which the glycan is attached: N-glycosylation, O-glycosylation and C-glycosylation. Synthesis of N-glycoproteins occurs in the rough endoplasmic reticulum (rER), and all N-glycoproteins synthesized in rER have uniform glycan endings with mannose (Man) and glucose (Glc). A systematic strategy was developed to comprehensiv... |
| Keywords: | glycosylation rER lectin affinity chromatography ConA LTQ-FT MS |
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