中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis

文献类型:期刊论文

作者Zhou, Houjiang; Tian, Ruijun; Ye, Mingliang; Xu, Songyun; Feng, Shun; Pan, Chensong; Jiang, Xiaogang; Li, Xin; Zou, Hanfa
刊名electrophoresis
出版日期2007-07-01
卷号28期号:13页码:2201-2215
关键词MALDI-TOF MS nano-LC MS/MS phosphopeptides phosphoproteome analysis zirconium dioxide nanoparticles
ISSN号0173-0835
产权排序1;1
通讯作者邹汉法
英文摘要large-scale characterization of phosphoproteins requires highly specific methods for the purification of phosphopeptides because of the low abundance of phosphoproteins and substoichiometry of phosphorylation. a phosphopeptide enrichment method using zro2 nanoparticles is presented. the high specificity of this approach was demonstrated by the isolation of phosphopeptides from the digests of model phosphoproteins. the strong affinity of zro2 nanoparticles to phosphopeptides enables the specific enrichment of phosphopeptides from a complex peptide mixture in which the abundance of phosphopeptides is two orders of magnitude lower than that of nonphosphopeptides. superior selectivity of zro2 nanoparticles for the enrichment of phosphorylated peptides than that of conventional immobilized metal affinity chromatography was observed. femtomole phosphopeptides from digestion products could be enriched by zro2 nanoparticles and can be well detected by maldi mass spectrometric analysis. zro2 nanoparticles were further applied to selectively isolate phosphopeptides from the tryptic digestion of mouse liver lysate for phosphoproteome analysis by nanoliter lc ms/ms (nano-lc-ms/ms) and ms/ms/ms. a total of 248 defining phosphorylation sites and 140 phosphorylated peptides were identified by manual validation using a series of rigid criteria.
WOS标题词science & technology ; life sciences & biomedicine ; physical sciences
类目[WOS]biochemical research methods ; chemistry, analytical
研究领域[WOS]biochemistry & molecular biology ; chemistry
关键词[WOS]mass-spectrometry ; affinity-chromatography ; phosphorylated proteins ; tyrosine phosphorylation ; posttranslational modifications ; surface-properties ; proteomic analysis ; ms analysis ; lc-ms/ms ; identification
收录类别SCI
原文出处true
语种英语
WOS记录号WOS:000248190400010
公开日期2010-11-30
源URL[http://159.226.238.44/handle/321008/98655]  
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Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Dalian 116023, Peoples R China
推荐引用方式
GB/T 7714
Zhou, Houjiang,Tian, Ruijun,Ye, Mingliang,et al. Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis[J]. electrophoresis,2007,28(13):2201-2215.
APA Zhou, Houjiang.,Tian, Ruijun.,Ye, Mingliang.,Xu, Songyun.,Feng, Shun.,...&Zou, Hanfa.(2007).Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis.electrophoresis,28(13),2201-2215.
MLA Zhou, Houjiang,et al."Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis".electrophoresis 28.13(2007):2201-2215.

入库方式: OAI收割

来源:大连化学物理研究所

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