Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography
文献类型:期刊论文
作者 | Han, Guanghui1; Ye, Mingliang1; Zhou, Houjiang1; Jiang, Xinning1; Feng, Shun1; Jiang, Xiaogang1; Tian, Ruijun1; Wan, Dafang2; Zou, Hanfa1; Gu, Jianren2 |
刊名 | proteomics
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出版日期 | 2008-04-01 |
卷号 | 8期号:7页码:1346-1361 |
关键词 | human liver phosphopeptide validation phosphoproteome analysis SAX |
ISSN号 | 1615-9853 |
产权排序 | 1;1 |
通讯作者 | 邹汉法 |
英文摘要 | the 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%. |
WOS标题词 | science & technology ; life sciences & biomedicine |
类目[WOS] | biochemical research methods ; biochemistry & molecular biology |
研究领域[WOS] | biochemistry & molecular biology |
关键词[WOS] | ion affinity-chromatography ; tandem mass-spectrometry ; protein identification technology ; titanium-dioxide microcolumns ; growth-factor receptor ; in-vivo ; tyrosine phosphorylation ; saccharomyces-cerevisiae ; signaling pathways ; membrane-proteins |
收录类别 | SCI |
原文出处 | true |
语种 | 英语 |
WOS记录号 | WOS:000254986200002 |
公开日期 | 2010-11-30 |
源URL | [http://159.226.238.44/handle/321008/99953] ![]() |
专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
作者单位 | 1.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 |
推荐引用方式 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.,...&Gu, Jianren.(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. |
入库方式: OAI收割
来源:大连化学物理研究所
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