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Quantitative interaction proteomics using mass spectrometry.
Journal article

Quantitative interaction proteomics using mass spectrometry.

  • Wepf A Institute of Molecular Systems Biology, Swiss Federal Institute of Technology, Eidgenössische Technische Hochschule Zürich, Wolfgang Pauli-Strasse 16, Zurich, Switzerland.
  • Glatter T
  • Schmidt A
  • Aebersold R
  • Gstaiger M
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  • 2009-02-10
Published in:
  • Nature methods. - 2009
Affinity Labels
Carboxylic Ester Hydrolases
Cell Line
Chromatography, Affinity
Chromatography, Liquid
Humans
Mass Spectrometry
Multiprotein Complexes
Okadaic Acid
Peptides
Phosphoprotein Phosphatases
Protein Interaction Mapping
Protein Phosphatase 2
Proteomics
Staining and Labeling
Tandem Mass Spectrometry
Transfection
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/123690
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