title: Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification.
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.
authors.affiliation: Institut für Pharmazeutische Chemie, Biozentrum, Universität Frankfurt, Frankfurt am Main, Germany.
authors.forename: Isam
authors.initials: I
authors.lastname: Rais
authors.forename: Michael
authors.initials: M
authors.lastname: Karas
authors.forename: Hermann
authors.initials: H
authors.lastname: Schägger
mesh_terms: D000818:Animals; D002417:Cattle; D019069:Cell Respiration; D015180:Electrophoresis, Gel, Two-Dimensional / Q000295:instrumentation / Q000379:methods*; D013058:Mass Spectrometry / Q000379:methods*; D008565:Membrane Proteins / Q000032:analysis* / Q000302:isolation & purification*; D024101:Mitochondrial Proteins / Q000032:analysis* / Q000302:isolation & purification*
chemical_list: D008565:Membrane Proteins; D024101:Mitochondrial Proteins