title: Separation of low molecular weight proteins with SDS-PAGE using taurine as a new trailing ion.
abstract: Taurine as an alternative trailing ion for tricine yields an identical resolution but reduces the running time by 15% and the power consumption by 15% compared to tricine. Therefore cooling of gels is more effective in SDS PAGE with taurine and artefacts due to oxidation of proteins can thus be reduced.
authors.affiliation: Department of Medicine II, Medical University of Lübeck, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Ehlermann
authors.forename: U
authors.initials: U
authors.lastname: Redweik
authors.forename: N
authors.initials: N
authors.lastname: Blau
authors.forename: C W
authors.initials: CW
authors.lastname: Heizmann
authors.forename: H A
authors.initials: HA
authors.lastname: Katus
authors.forename: A
authors.initials: A
authors.lastname: Remppis
mesh_terms: D016477:Artifacts; D002021:Buffers; D002135:Calcium-Binding Proteins / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005782:Gels; D005998:Glycine / Q000031:analogs & derivatives*; D007202:Indicators and Reagents; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D013654:Taurine
chemical_list: D002021:Buffers; D002135:Calcium-Binding Proteins; D005782:Gels; D007202:Indicators and Reagents; D011506:Proteins; D013654:Taurine; D005998:Glycine; C100184:tricine