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

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Abstract
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.