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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