Separated by differing electrophoretic mobilities, analytes migrate toward the electrode of opposite charge. Changes in enzyme restriction, electrophoretic and chromatographic profiles can be measured. Gliadins are prolamins and are separated on the basis of electrophoretic mobility and isoelectric focusing. The kinetics of electrophoretic deposition are mostly examined for planar geometries. However, non-aqueous electrophoretic deposition applications are known. SDS-PAGE is generally used for the denaturing electrophoretic separation of proteins. As for all electrophoretic techniques, it is most appropriate for charged analytes. The pH of an electrophoretic gel is determined by the buffer used for that gel. SDS-PAGE is the most widely used method for gel electrophoretic separation of proteins. These methods include microelectrophoresis, electrophoretic light scattering and electroacoustics. These displays are constructed from an electrophoretic imaging film manufactured by E Ink Corporation. From the inverse translocation time versus voltage-dependent electrophoretic mobility, and thus zeta potentials are calculated. In 1937, Arne Tiselius developed the first sophisticated electrophoretic apparatus. Anionic dyes of a known electrophoretic mobility are usually included in the sample buffer. Immunofixation identifies antibodies in a mixture as a function of their specific electrophoretic mobility.