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Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis
Zhou, Houjiang; Tian, Ruijun; Ye, Mingliang; Xu, Songyun; Feng, Shun; Pan, Chensong; Jiang, Xiaogang; Li, Xin; Zou, Hanfa; Zou HF(邹汉法); Zou HF(邹汉法)
KeywordMaldi-tof Ms Nano-lc Ms/ms Phosphopeptides Phosphoproteome Analysis Zirconium Dioxide Nanoparticles
Source PublicationELECTROPHORESIS
2007-07-01
ISSN0173-0835
DOI10.1002/elps.200600718
Volume28Issue:13Pages:2201-2215
Indexed BySCI
SubtypeArticle
Department18
Funding Project1809
Contribution Rank1;1
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS KeywordMASS-SPECTROMETRY ; AFFINITY-CHROMATOGRAPHY ; PHOSPHORYLATED PROTEINS ; TYROSINE PHOSPHORYLATION ; POSTTRANSLATIONAL MODIFICATIONS ; SURFACE-PROPERTIES ; PROTEOMIC ANALYSIS ; MS ANALYSIS ; LC-MS/MS ; IDENTIFICATION
AbstractLarge-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.
Language英语
URL查看原文
WOS IDWOS:000248190400010
Citation statistics
Cited Times:130[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/98655
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)
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Dalian 116023, Peoples R China
Recommended Citation
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.,...&邹汉法.(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.
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