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Counteracting chromatographic electrophoresis (CACE) uses opposing electric and convective fields to focus proteins at the boundary separating distinct granular gel phases. In batch operation, CACE can purify, stack, and concentrate gram quantities of proteins. This technique has been extended to continuous operation by modifying the batch column. Experiments were then used to demonstrate operation of the column. The principles underlying focusing and separation are elucidated by linear chromatography theory.

Recycle continuous-flow electrophoresis (RCFE) is a modification of Hannig's thin-film CFE device in which eluant is continuously recycled to the chamber inlet. Shifting the recycled eluent laterally a specific distance prior to reinjection enables the RCFE to separate any two solutes to arbitrary purity. This paper studies solute transport in an idealized RCFE in the absence of diffusion. The model is solved analytically by means of a two-sided Laplace transform. Three distinct types of solute distribution are found, and guidelines for construction and operation of an RCFE are derived.

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Continuous free-flow electrophoresis (CFE) provides the biochemist with a powerful technique for preparative-scale purification of labile biomolecules. However, solute resolution in the classic CFE is limited by the deleterious effects of diffusion, electroosmotic dispersion, and connective dispersion. These problems can be overcome in the CFE by continuously recycling effluent through the chamber in a manner which allows complete recovery of undiluted product at arbitrarily high purities.Mathematical models of the continuous flow device with recycle (RCFE) are derived for the two limiting cases: rapid diffusion and slow diffusion. The analytical solutions of these models are used to predict separation factors under various operating conditions.