Use of selected reaction monitoring data for label-free quantification of protein modification stoichiometry

Proteomics. 2010 Dec;10(23):4301-5. doi: 10.1002/pmic.201000232.

Abstract

Quantification of protein and PTM abundance in biological samples is an important component of proteomic studies. Label-free methods for quantification using MS are attractive because they are simple to implement and applicable to any experimental system. We demonstrate that PTM stoichiometry can be accurately measured using label-free quantification and selected reaction monitoring. Use of selected reaction monitoring is advantageous with complex biological samples and we show this approach can be used to quantify multiple PTMs independently on a single peptide.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cell Extracts
  • Fungal Proteins / chemistry
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Phosphopeptides / chemistry*
  • Phosphorylation
  • Proteins / chemistry*
  • Proteomics / methods
  • Receptor, EphA2 / chemistry
  • Recombinant Proteins / chemistry

Substances

  • Cell Extracts
  • Fungal Proteins
  • Peptide Fragments
  • Phosphopeptides
  • Proteins
  • Recombinant Proteins
  • Receptor, EphA2