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Open Access Green as soon as Postprint is submitted to ZB.
Two-dimensional electrophoresis of membrane proteins.
Anal. Bioanal. Chem. 389, 1033-1045 (2007)
One third of all genes of various organisms encode membrane proteins, emphasizing their crucial cellular role. However, due to their high hydrophobicity, membrane proteins demonstrate low solubility and a high tendency for aggregation. Indeed, conventional two-dimensional gel electrophoresis (2-DE), a powerful electrophoretic method for the separation of complex protein samples that applies isoelectric focusing (IEF) in the first dimension and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in the second dimension, has a strong bias against membrane proteins. This review describes two-dimensional electrophoretic techniques that can be used to separate membrane proteins. Alternative methods for performing conventional 2-DE are highlighted; these involve replacing the IEF with electrophoresis using cationic detergents, namely 16-benzyldimethyl-n-hexadecylammonium chloride (16-BAC) and cetyl trimethyl ammonium bromide (CTAB), or the anionic detergent SDS. Finally, the separation of native membrane protein complexes through the application of blue and clear native gel electrophoresis (BN/CN-PAGE) is reviewed, as well as the free-flow electrophoresis (FFE) of membranes.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Membrane proteins; SDS/SDS-PAGE; 16-BAC/SDS-PAGE; BN-PAGE ; Free-flow electrophoresis
ISSN (print) / ISBN
1618-2642
e-ISSN
1618-2650
Quellenangaben
Volume: 389,
Issue: 4,
Pages: 1033-1045
Publisher
Springer
Publishing Place
Heidelberg
Reviewing status
Peer reviewed
Institute(s)
Institute of Human Genetics (IHG)