1997/01/01 by Thierry Rabilloud, T. Rabilloud, C. Adessi +5 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Engineering · #Analytical Chemistry and Chromatography #Nanopore and Nanochannel Transport Studies #Protein Structure and Dynamics #q-bio.GN
paper · pdf · doi:10.1002/elps.1150180303
published as Electrophoresis 18 (31/03/1997) 307-16 · website publisher: http://www.interscience.wiley.com
openalex publication_date 1997/01/01 · arxiv created 2006/12/04 · arxiv updated 2009/12/01 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/28
Membrane and nuclear proteins of poor solubility have been separated by high resolution two-dimensional (2-D) gel electrophoresis. Isoelectric focusing with immobilized pH gradients leads to severe quantitative losses of proteins in the resulting 2-D map, although the resolution is usually high. Protein solubility could be improved by using denaturing solutions containing various detergents and chaotropes. Best results were obtained with a denaturing solution containing urea, thiourea, and detergents (both nonionic and zwitterionic). The usefulness of thiourea-containing denaturing mixtures is shown for microsomal and nuclear proteins as well as for tubulin, a protein highly prone to aggregation.