Advances in protein solubilisation for two-dimensional electrophoresis

Ben Herbert*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Two-dimensional (2-D) electrophoresis remains the highest resolution technique tor protein separation and is the method of choice when complex samples need to be arrayed for characterisation, as in proteomics. However, in current proteome projects the total number of proteins identified from 2-D gels is often only a small percentage of the predicted proteome. In addition, there is an almost complete lack of hydrophobic proteins on 2-D gels, especially those using immobilised pH gradients. Recently there have been a number of publications reporting reagents which improve protein solubilisation prior to isoelectric focusing. The improved solubilization possible with these reagents has increased the total number of proteins able to be visualised on 2-D gels and also allowed the separation of hydrophobic proteins, such as integral membrane proteins.

Original languageEnglish
Title of host publicationFrom genome to proteome
Subtitle of host publicationadvances in the practice & application of proteomics
EditorsMichael Dunn
Place of PublicationWeinheim, Germany
PublisherWiley-Blackwell, Wiley
Pages80-83
Number of pages4
ISBN (Electronic)9783527613489
ISBN (Print)9783527301546
DOIs
Publication statusPublished - 26 Dec 2007

Keywords

  • Membrane proteins
  • Proteome
  • Review
  • Solubility
  • Two-dimensional Polyacrylamide gel electrophoresis

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