Brief Communication abstract
Nature Methods 6, 203 - 205 (2009)
Published online: 8 February 2009 | doi:10.1038/nmeth.1302
Quantitative interaction proteomics using mass spectrometry
Alexander Wepf1,2, Timo Glatter1,2, Alexander Schmidt1,2, Ruedi Aebersold1,2,3,4 & Matthias Gstaiger1,2
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.
- Institute of Molecular Systems Biology, Swiss Federal Institute of Technology, Eidgenössische Technische Hochschule Zürich, Wolfgang Pauli-Str. 16, CH-8093 Zurich, Switzerland.
- Competence Center for Systems Physiology and Metabolic Diseases, Schafmattstr. 18, CH-8093 Zurich, Switzerland.
- Faculty of Science, University of Zurich, Winterthurerstr. 190, CH-8057 Zurich, Switzerland.
- Institute of Systems Biology, 1441 North 34th Street, Seattle, Washington 98103, USA.
Correspondence to: Matthias Gstaiger1,2 e-mail: gstaiger@imsb.biol.ethz.ch
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