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Cited by 459

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

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Rabilloud, Thierry, Adessi, Céline, Giraudel, Anne, Lunardi, Joël·1997·ELECTROPHORESIS

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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Metadata

Authors
Rabilloud, T., Adessi, C., Giraudel, A., & Lunardi, J.
Venue
ELECTROPHORESIS
Publisher
Wiley
Published
1997-01
Volume
18
Issue
3-4
Pages
307-316
ISSN
  • 0173-0835 (ISSN-L)
  • 1522-2683
OpenAlex
W2130381045
Cited by
459
References
1
FWCI
20.13
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Improvement of the solubilization of proteins in two‐dimensional electrophoresis with immobilized pH gradients. https://app.cochat.ai/papers/10.1002/elps.1150180303
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Rabilloud, T., Adessi, C., Giraudel, A., & Lunardi, J. (1997). Improvement of the solubilization of proteins in two‐dimensional electrophoresis with immobilized pH gradients. ELECTROPHORESIS. https://doi.org/10.1002/elps.1150180303

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