Two-dimensional separation of membrane proteins by 16-BAC-SDS-PAGE.
Defining membrane proteomes is fundamental to our understanding of many physiological and pathophysiological processes. Their separation and identification is hence a key issue in basic and biomedical research. Due to their hydrophobic character, few high-resolution techniques for separation are available for qualitative and quantitative approaches. For gel-based methods, the two-dimensional 16-BAC/SDS-PAGE is the method of choice. This technique separates proteins in the first dimension using an acidic buffer system and the cationic detergent benzyldimethyl-n-hexadecylammonium chloride (16-BAC) and in the second dimension by SDS-PAGE. Here, we describe a detailed protocol for the separation of proteins by 16-BAC/SDS-PAGE.
Nothwang
Hans Gerd
HG
Abteilung Neurogenetik, Institut für Biologie und Umweltwissenschaften, Oldenburg, Germany.
Schindler
Jens
J
D002021:Buffers; D005591:Chemical Fractionation / Q000379:methods*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005233:Fatty Alcohols; D008565:Membrane Proteins / Q000302:isolation & purification*; D000644:Quaternary Ammonium Compounds / Q000737:chemistry*
D002021:Buffers; D005233:Fatty Alcohols; D008565:Membrane Proteins; D000644:Quaternary Ammonium Compounds; C012817:cetalkonium chloride