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Fractionation of phosphopeptides on strong anion-exchange capillary trap column for large-scale phosphoproteome analysis of microgram samples
Wang, Fangjun; Han, Guanghui; Yu, Zhiyuan; Jiang, Xinning; Sun, Shutao; Chen, Rui; Ye, Mingliang; Zou, Hanfa; Zou HF(邹汉法)
KeywordFractionating Human Liver Phosphoproteome Strong Anion-exchange Trap Column
Source PublicationJOURNAL OF SEPARATION SCIENCE
2010-07-01
ISSN1615-9306
DOI10.1002/jssc.200900718
Volume33Issue:13Pages:1879-1887
Indexed BySCI
SubtypeArticle
Department18
Funding Project1809
Contribution Rank1;1
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordSPECTROMETRY-BASED PROTEOMICS ; ION AFFINITY-CHROMATOGRAPHY ; LC-MS/MS ANALYSIS ; PHOSPHORYLATED PEPTIDES ; MASS-SPECTROMETRY ; POSTTRANSLATIONAL MODIFICATIONS ; MAGNETIC NANOPARTICLES ; LIQUID-CHROMATOGRAPHY ; SHOTGUN PROTEOMICS ; MOUSE-LIVER
AbstractIt is one of the key issues to develop powerful fractionating method to increase the identification of the low-abundance phosphopeptides. In this study, a semi-online 2-D LC separation strategy based on three-step fractionation of the enriched peptides on strong anion-exchange trap column was developed. It was demonstrated that the sensitivity and phosphoproteome coverage obtained by this fractionating method with strong anion-exchange trap column is much higher than those by the conventional methods based on C18 trap column. In addition, when the same amount of sample was loaded, the number of identified phosphopeptides had increased 108%. Combination of this three-step fractionation method with RPLC-MS/MS analysis by 300 min RP-gradient separation was applied to phosphoproteome analysis of human liver proteins, and 853 unique phosphopeptides was positively identified from 500 mu g tryptic digest of human liver proteins. After three cycles' consecutive analyses, 1554 unique phosphopeptides and 1566 phosphorylated sites were totally identified from 735 phosphorylated proteins at a false discovery rate of < 1% in about 54h of analysis time.
Language英语
URL查看原文
WOS IDWOS:000280163900001
Citation statistics
Cited Times:15[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/103147
Collection中国科学院大连化学物理研究所
Corresponding AuthorZou HF(邹汉法)
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Wang, Fangjun,Han, Guanghui,Yu, Zhiyuan,et al. Fractionation of phosphopeptides on strong anion-exchange capillary trap column for large-scale phosphoproteome analysis of microgram samples[J]. JOURNAL OF SEPARATION SCIENCE,2010,33(13):1879-1887.
APA Wang, Fangjun.,Han, Guanghui.,Yu, Zhiyuan.,Jiang, Xinning.,Sun, Shutao.,...&邹汉法.(2010).Fractionation of phosphopeptides on strong anion-exchange capillary trap column for large-scale phosphoproteome analysis of microgram samples.JOURNAL OF SEPARATION SCIENCE,33(13),1879-1887.
MLA Wang, Fangjun,et al."Fractionation of phosphopeptides on strong anion-exchange capillary trap column for large-scale phosphoproteome analysis of microgram samples".JOURNAL OF SEPARATION SCIENCE 33.13(2010):1879-1887.
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