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Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography
Han, Guanghui1; Ye, Mingliang1; Zhou, Houjiang1; Jiang, Xinning1; Feng, Shun1; Jiang, Xiaogang1; Tian, Ruijun1; Wan, Dafang2; Zou, Hanfa1; Gu, Jianren2; Zou HF(邹汉法); Zou HF(邹汉法)
KeywordHuman Liver Phosphopeptide Validation Phosphoproteome Analysis Sax
Source PublicationPROTEOMICS
2008-04-01
ISSN1615-9853
DOI10.1002/pmic.200700884
Volume8Issue:7Pages:1346-1361
Indexed BySCI
SubtypeArticle
Department18
Funding Project1809
Contribution Rank1;1
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordION AFFINITY-CHROMATOGRAPHY ; TANDEM MASS-SPECTROMETRY ; PROTEIN IDENTIFICATION TECHNOLOGY ; TITANIUM-DIOXIDE MICROCOLUMNS ; GROWTH-FACTOR RECEPTOR ; IN-VIVO ; TYROSINE PHOSPHORYLATION ; SACCHAROMYCES-CEREVISIAE ; SIGNALING PATHWAYS ; MEMBRANE-PROTEINS
AbstractThe mixture of phosphopeptides enriched from proteome samples are very complex. To reduce the complexity it is necessary to fractionate the phosphopeptides. However, conventional enrichment methods typically only enrich phosphopeptides but not fractionate phosphopeptides. In this study, the application of strong anion exchange (SAX) chromatography for enrichment and fractionation of phosphopeptides was presented. it was found that phosphopeptides were highly enriched by SAX and majority of unmodified peptides did not bind onto SAX. Compared with Fe3+ immobilized metal affinity chromatography (Fe3+-IMAC), almost double phosphopeptides were identified from the same sample when only one fraction was generated by SAX. SAX and Fe3+-IMAC showed the complementarity in enrichment and identification of phosphopeptides. It was also demonstrated that SAX have the ability to fractionate phosphopeptides under gradient elution based on their different interaction with SAX adsorbent. SAX was further applied to enrich and fractionate phosphopeptides in tryptic digest of proteins extracted from human liver tissue adjacent to tumorous region for phosphoproteome profiling. This resulted in the highly confident identification of 274 phosphorylation sites from 305 unique phosphopeptides corresponding to 168 proteins at false discovery rate (FDR) of 0.96%.
Language英语
URL查看原文
WOS IDWOS:000254986200002
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Cited Times:149[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/99953
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 R&A Ctr, Dalian 116023, Peoples R China
2.Shanghai Canc Inst, State Key Lab Oncogenes & Related Genes, Shanghai, Peoples R China
Recommended Citation
GB/T 7714
Han, Guanghui,Ye, Mingliang,Zhou, Houjiang,et al. Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography[J]. PROTEOMICS,2008,8(7):1346-1361.
APA Han, Guanghui.,Ye, Mingliang.,Zhou, Houjiang.,Jiang, Xinning.,Feng, Shun.,...&邹汉法.(2008).Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.PROTEOMICS,8(7),1346-1361.
MLA Han, Guanghui,et al."Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography".PROTEOMICS 8.7(2008):1346-1361.
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