Elimination of protein band "edge tailing" in Weber-Osborn-type slab gel electrophoresis by glycerol.
In sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) according to the method of Weber and Osborn, protein bands are often distorted by tailing at both ends, and the phenomenon is often called "edge tailing." This was eliminated by adding glycerol at a concentration of 10-15% (v/v) to the sample-well gel supplemented to form the sample wells. This simple modification made the protein bands as sharp and straight as those in SDS-PAGE according to the Laemmli procedure. The linearity of the semilogarithmic plot of mobilities versus molecular mass was better than that obtained by Laemmli-type SDS-PAGE.
Kubo
K
K
Faculty of Pharmaceutical Sciences, Kinki University, Osaka, Japan.
D003574:Cytochrome c Group / Q000032:analysis / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D005990:Glycerol; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification*; D012394:Rosaniline Dyes; D012967:Sodium Dodecyl Sulfate
D003574:Cytochrome c Group; D011506:Proteins; D012394:Rosaniline Dyes; C005095:malachite green; D012967:Sodium Dodecyl Sulfate; C024757:Coomassie brilliant blue R; D005990:Glycerol