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

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dc.creatorRabilloud, T.
dc.creatorAdessi, C.
dc.creatorGiraudel, A.
dc.creatorLunardi, J.
dc.date2006-12-04
dc.date.accessioned2026-07-07T07:35:02Z
dc.date.available2026-07-07T07:35:02Z
dc.descriptionMembrane 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.
dc.descriptionwebsite publisher: http://www.interscience.wiley.com
dc.identifierhttps://arxiv.org/abs/q-bio/0612002
dc.identifierhttp://arxiv.org/abs/q-bio/0612002
dc.identifierElectrophoresis 18 (31/03/1997) 307-16
dc.identifierdoi:10.1002/elps.1150180303
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/119973
dc.subjectGenomics
dc.titleImprovement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
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