Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification

Proteomics. 2004 Sep;4(9):2567-71. doi: 10.1002/pmic.200400829.


Acrylamide concentration, urea content, and the trailing ion used for sodium dodecyl sulfate (SDS)-gels modify electrophoretic protein mobilities in a protein-dependent way. Varying these parameters we coupled two SDS-gels to a two-dimensional (2-D) electrophoresis system. Protein spots in 2-D gels are dispersed around a diagonal. Hydrophobic proteins are well separated from water-soluble proteins which is the essential advantage of the novel technique. Mass spectrometric identification of previously unaccessible hydrophobic proteins is now possible.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cell Respiration
  • Electrophoresis, Gel, Two-Dimensional / instrumentation
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Mass Spectrometry / methods*
  • Membrane Proteins / analysis*
  • Membrane Proteins / isolation & purification*
  • Mitochondrial Proteins / analysis*
  • Mitochondrial Proteins / isolation & purification*


  • Membrane Proteins
  • Mitochondrial Proteins