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题名: Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
作者: Feng, Shun;  Ye, Mingliang;  Zhou, Houjiang;  Jiang, Xiaogang;  Jiang, Xingning;  Zou, Hanfa;  Gong, Bolin
通讯作者: 邹汉法
刊名: MOLECULAR & CELLULAR PROTEOMICS
发表日期: 2007-09-01
DOI: 10.1074/mcp.T600071-MCP200
卷: 6, 期:9, 页:1656-1665
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1809
产权排名: 1;1
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemical Research Methods
研究领域[WOS]: Biochemistry & Molecular Biology
英文摘要: Large scale characterization of phosphoproteins requires highly specific methods for purification of phosphopeptides because of the low abundance of phosphoproteins and substoichiometry of phosphorylation. Enrichment of phosphopeptides from complex peptide mixtures by IMAC is a popular way to perform phosphoproteome analysis. However, conventional IMAC adsorbents with iminodiacetic acid as the chelating group to immobilize Fe3+ lack enough specificity for efficient phosphoproteome analysis. Here we report a novel IMAC adsorbent through Zr4+ chelation to the phosphonate- modified poly( glycidyl methacrylate- co- ethylene dimethacrylate) polymer beads. The high specificity of Zr4+- IMAC adsorbent was demonstrated by effectively enriching phosphopeptides from the digest mixture of phosphoprotein (alpha- or beta- casein) and bovine serum albumin with molar ratio at 1: 100. Zr(4 +)IMAC adsorbent was also successfully applied for the analysis of mouse liver phosphoproteome, resulting in the identification of 153 phosphopeptides ( 163 phosphorylation sites) from 133 proteins in mouse liver lysate. Significantly more phosphopeptides were identified than by the conventional Fe3+- IMAC approach, indicating the excellent performance of the Zr4 IMAC approach. The high specificity of Zr4+- IMAC adsorbent was found to mainly result from the strong interaction between chelating Zr4+ and phosphate group on phosphopeptides. Enrichment of phosphopeptides by Zr4 +- IMAC provides a powerful approach for large scale phosphoproteome analysis.
关键词[WOS]: TANDEM MASS-SPECTROMETRY ;  PROTEIN-PHOSPHORYLATION ANALYSIS ;  LARGE-SCALE ANALYSIS ;  TYROSINE PHOSPHORYLATION ;  SELECTIVE ENRICHMENT ;  MONOLITHIC CAPILLARY ;  YEAST PROTEOME ;  MS/MS ANALYSIS ;  LC-MS/MS ;  IDENTIFICATION
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000249237200015
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/98729
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog Res & Anal Ctr, Dalian 116023, Peoples R China
2.Xinjiang Univ, Coll Chem & Chem Engn, Urumqi 830046, Xinjiang, Peoples R China
3.Ningxia Univ, Key Lab Biotechnol, Yin Chuan 750021, Peoples R China

Recommended Citation:
Feng, Shun,Ye, Mingliang,Zhou, Houjiang,et al. Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis[J]. MOLECULAR & CELLULAR PROTEOMICS,2007,6(9):1656-1665.
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