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Published on: November 26, 2008
Separation of membrane proteins by two-dimensional electrophoresis using cationic rehydrated strips
Birger Wenge1, Heinz Bönisch, Julia Grabitzki
1Institute of Pharmacology and Toxicology, University of Bonn, Bonn, Germany.
Abstract:
Due to their poor solubility during IEF membrane proteins cannot be separated and analyzed satisfactorily with classical 2-DE. A more efficient method for such hydrophobic proteins is the benzyldimethyl-n-hexadecylammonium chloride (16-BAC)/SDS-PAGE, but the corresponding protocol is intricate and time-consuming. We now developed an easy-to-handle electrophoresis method in connection with a novel device which enables reproducible separation of ionic solubilized membrane proteins using individually rehydrated plastic sheet gel strips. These strips are suitable for the first dimension in a 2-D 16-BAC/SDS system and can be handled easily; this is demonstrated by the separation of membrane proteins of human embryonic kidney (HEK293) cells.
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