Polyacrylamide gel electrophoresis of wheat gliadins: the use of a moving boundary for improved resolution

The process of the separation of gliadin proteins of wheat, using polyacrylamide gel electrophoresis, was studied in detail. It was shown that electrophoresis is a dynamic process during which the pH of the gel changes together with the potassium ion concentration. The most positive effect on the separation of the gliadins was generated by a moving front, which is a boundary between regions with a low concentration of K super(+) ions and a low pH, and region with a high concentration of K super(+) ions and a high pH, after optimization of the concentrations of the cations and anions in the electrode solutions. The finding was exploited for the development of an extremely simple electrophoresis system, in which buffers were not needed for obtaining a high resolution. The system was further improved by applying a stacking gel. The advantages of this system are discussed. This new approach may be useful for improving electrophoresis systems for other applications.