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Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients

T. Rabilloud·C. Adessi·A. Giraudel·J. Lunardi
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Abstract

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.

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T. Rabilloud, C. Adessi, A. Giraudel, J. Lunardi. 2006-12-04. Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. https://doi.org/10.1002/elps.1150180303

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