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

Author(s): Rais I, Karas M, Schgger H

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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. This article was published in Proteomics and referenced in

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