Quantitative interaction proteomics using mass spectrometry

被引：0

作者：

Wepf, Alexander ^{[1
,2
]}

Glatter, Timo ^{[1
,2
]}

Schmidt, Alexander ^{[1
,2
]}

Aebersold, Ruedi ^{[1
,2
,3
,4
]}

Gstaiger, Matthias ^{[1
,2
]}

机构：

[1] ETH, Swiss Fed Inst Technol, Inst Mol Syst Biol, CH-8093 Zurich, Switzerland

[2] Competence Ctr Syst Physiol & Metab Dis, CH-8093 Zurich, Switzerland

[3] Univ Zurich, Fac Sci, CH-8057 Zurich, Switzerland

[4] Inst Syst Biol, Seattle, WA 98103 USA

来源：

NATURE METHODS | 2009年 / 6卷 / 03期

基金：

美国国家卫生研究院;

关键词：

PROTEIN PHOSPHATASE 2A; QUANTIFICATION; PEPTIDES;

D O I：

10.1038/NMETH.1302

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We present a mass spectrometry-based strategy for the absolute quantification of protein complex components isolated through affinity purification. We quantified bait proteins via isotope-labeled reference peptides corresponding to an affinity tag sequence and prey proteins by label-free correlational quantification using the precursor ion signal intensities of proteotypic peptides generated in reciprocal purifications. We used this method to quantitatively analyze interaction stoichiometries in the human protein phosphatase 2A network.

引用

页码：203 / 205

页数：3

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