Separation of low molecular weight proteins with SDS-PAGE using taurine as a new trailing ion

P Ehlermann; U Redweik; N Blau; C W Heizmann; H A Katus; A Remppis

Separation of low molecular weight proteins with SDS-PAGE using taurine as a new trailing ion

Gen Physiol Biophys. 2001 Jun;20(2):203-7.

Authors

P Ehlermann¹, U Redweik, N Blau, C W Heizmann, H A Katus, A Remppis

Affiliation

¹ Department of Medicine II, Medical University of Lübeck, Germany.

PMID: 11519691

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.

Publication types

Comparative Study

MeSH terms

Artifacts
Buffers
Calcium-Binding Proteins / isolation & purification
Electrophoresis, Polyacrylamide Gel / methods
Gels
Glycine / analogs & derivatives*
Indicators and Reagents
Molecular Weight
Oxidation-Reduction
Proteins / chemistry
Proteins / isolation & purification*
Taurine*

Substances

Buffers
Calcium-Binding Proteins
Gels
Indicators and Reagents
Proteins
Taurine
Glycine
tricine