Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry
文献类型：期刊论文
| 作者 | Jin, WH; Dai, J; Zhou, H; Xia, QC; Zou, HF; Zeng, R |
| 刊名 | rapid communications in mass spectrometry
 |
| 出版日期 | 2004 |
| 卷号 | 18期号:18页码:2169-2176 |
| 产权排序 | 2;1 |
| 英文摘要 | since protein phosphorylation is a dominant mechanism of information transfer in cells, there is a great need for methods capable of accurately elucidating sites of phosphorylation. in recent years mass spectrometry has become an increasingly viable alternative to more traditional methods of phosphorylation analysis. the present study used immobilized metal affinity chromatography (imac coupled with a linear ion trap mass spectrometer to analyze phosphorylated proteins in mouse liver. a total of 26 peptide sequences defining 26 sites of phosphorylation were determined. although this number of identified phosphoproteins is not large, the approach is still of interest because a series of conservative criteria were adopted in data analysis. we note that, although the binding of non-phosphorylated peptides to the imac column was apparent, the improvements in high-speed scanning and quality of ms/ms spectra provided by the linear ion trap contributed to the phosphoprotein identification. further analysis demonstrated that ms/ms/ms analysis was necessary to exclude the false-positive matches resulting from the ms/ms experiments, especially for multiphosphorylated peptides. the use of the linear ion trap considerably enabled exploitation of nanoflow-hplc/ms/ms, and in addition ms/ms/ms has great potential in phosphoproteome research of relatively complex samples. copyright (c) 2004 john wiley sons, ltd. |
| WOS标题词 | science & technology ; physical sciences ; technology |
| 类目[WOS] | chemistry, analytical ; spectroscopy |
| 研究领域[WOS] | chemistry ; spectroscopy |
| 关键词[WOS] | phospho-specific antibodies ; in-vivo phosphorylation ; protein-phosphorylation ; tyrosine phosphorylation ; functional proteomics ; sites ; identification ; calnexin ; chromatography ; enrichment |
| 收录类别 | SCI |
| 原文出处 | true |
| 语种 | 英语 |
| WOS记录号 | WOS:000223872700021 |
| 公开日期 | 2010-11-30 |
| 源URL | [http://159.226.238.44/handle/321008/81909]  |
| 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, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Res Ctr Proteome Anal,Key Lab Proteom, Shanghai 200031, Peoples R China 2.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Dalian 116011, Peoples R China |
| 推荐引用方式 GB/T 7714 | Jin, WH,Dai, J,Zhou, H,et al. Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry[J]. rapid communications in mass spectrometry,2004,18(18):2169-2176. |
| APA | Jin, WH,Dai, J,Zhou, H,Xia, QC,Zou, HF,&Zeng, R.(2004).Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry.rapid communications in mass spectrometry,18(18),2169-2176. |
| MLA | Jin, WH,et al."Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry".rapid communications in mass spectrometry 18.18(2004):2169-2176. |
入库方式： OAI收割
来源：大连化学物理研究所
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