FACTORS AFFECTING THE ELECTROPHORETIC MOBILITY OF THE MAJOR OUTER-MEMBRANE PROTEINS OF ESCHERICHIA-COLI IN POLYACRYLAMIDE GELS

The outer membrane proteins of Escherichia coli can be resolved by polyacrylamide gel electrophoresis in the presence of anionic detergents. Factors such as the choice of detergent and buffer system and the presence of urea in the separation gel are all shown to affect the charge and/or the configuration of the detergent-protein complexes and will affect the relative migration of these complexes to different extents. The procedures described in this paper may be of use in the determination of the relatedness of the proteins from the same or different strains. In addition, detailed examinations of the effects of these different parameters and the effect of changes in acrylamide concentrations may be useful in the detection of unusual characteristics which may indicate the presence of posttranslational modification. © 1979.