Stable isotope-coded proteomic mass spectrometry

Curr Opin Biotechnol. 2003 Feb;14(1):101-9. doi: 10.1016/s0958-1669(02)00014-9.


Developing the ability to quantify changes in protein abundance between cells subjected to a variety of physiological and environmental conditions is an extremely active area of proteome research. Although advances in chromatography, mass spectrometry instrumentation, and bioinformatics have contributed to producing a viable method for comparative proteome-wide analyses, the highest precision of quantitation is based, in part, upon improved methods for chemical and metabolic stable isotope labeling of proteins and peptides. The ability to quantify differences in protein expression and post-translational modifications using stable isotope labeling has been achieved, but insights into the biochemical mechanisms that will contribute to the development of new biotechnologies have yet to be realized.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Affinity Labels / chemical synthesis
  • Amino Acids
  • Gene Expression Profiling / methods*
  • Indicators and Reagents
  • Isotope Labeling / methods*
  • Mass Spectrometry / methods*
  • Nitrogen Isotopes
  • Oxygen Isotopes
  • Protein Biosynthesis
  • Proteins / analysis
  • Proteins / chemistry*
  • Proteins / genetics*
  • Proteins / metabolism
  • Proteome / analysis
  • Proteome / chemistry
  • Proteomics / methods*
  • Recombinant Proteins / analysis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics


  • Affinity Labels
  • Amino Acids
  • Indicators and Reagents
  • Nitrogen Isotopes
  • Oxygen Isotopes
  • Proteins
  • Proteome
  • Recombinant Proteins