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Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
Feng, Shun; Ye, Mingliang; Zhou, Houjiang; Jiang, Xiaogang; Jiang, Xingning; Zou, Hanfa; Gong, Bolin; Zou HF(邹汉法); Zou HF(邹汉法)
Source PublicationMOLECULAR & CELLULAR PROTEOMICS
2007-09-01
ISSN1535-9476
DOI10.1074/mcp.T600071-MCP200
Volume6Issue:9Pages:1656-1665
Indexed BySCI
SubtypeArticle
Department18
Funding Project1809
Contribution Rank1;1
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemical Research Methods
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordTANDEM MASS-SPECTROMETRY ; PROTEIN-PHOSPHORYLATION ANALYSIS ; LARGE-SCALE ANALYSIS ; TYROSINE PHOSPHORYLATION ; SELECTIVE ENRICHMENT ; MONOLITHIC CAPILLARY ; YEAST PROTEOME ; MS/MS ANALYSIS ; LC-MS/MS ; IDENTIFICATION
AbstractLarge 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.
Language英语
URL查看原文
WOS IDWOS:000249237200015
Citation statistics
Cited Times:201[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/98729
Collection中国科学院大连化学物理研究所
Corresponding AuthorZou HF(邹汉法); Zou HF(邹汉法)
Affiliation1.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
GB/T 7714
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.
APA Feng, Shun.,Ye, Mingliang.,Zhou, Houjiang.,Jiang, Xiaogang.,Jiang, Xingning.,...&邹汉法.(2007).Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis.MOLECULAR & CELLULAR PROTEOMICS,6(9),1656-1665.
MLA Feng, Shun,et al."Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis".MOLECULAR & CELLULAR PROTEOMICS 6.9(2007):1656-1665.
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