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Braun, R.J. ; Kinkl, N. ; Beer, M. ; Ueffing, M.

Two-dimensional electrophoresis of membrane proteins.

Anal. Bioanal. Chem. 389, 1033-1045 (2007)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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
Language english
Publication Year 2007
HGF-reported in Year 2007
ISSN (print) / ISBN 1618-2642
e-ISSN 1618-2650
Journal Analytical and Bioanalytical Chemistry
Quellenangaben Volume: 389, Issue: 4, Pages: 1033-1045 Article Number: , Supplement: ,
Publisher Springer
Publishing Place Heidelberg
Reviewing status Peer reviewed
Institute(s) Institute of Human Genetics (IHG)
Research field(s) Genetics and Epidemiology
PSP Element(s) FE 70722
PubMed ID 17680235
DOI 10.1007/s00216-007-1514-6
Scopus ID 34748866570
Erfassungsdatum 2007-09-07
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