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Proteomics. 2004 Sep;4(9):2567-71.

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

Author information

1
Institut für Pharmazeutische Chemie, Biozentrum, Universität Frankfurt, Frankfurt am Main, Germany.

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.

PMID:
15352231
DOI:
10.1002/pmic.200400829
[Indexed for MEDLINE]

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