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The renewed interest in the preparative ap plications of electrophoretic techniques is due to the demands of the rapidly emerg ing biotechnology industry for large scale protein purification methods. This interest is exemplified by NASA' s recent establishment of two university based centers of excellence in separation science as well as by the Elec trophoresis Operations in Space program of the McDonnell Douglas Corporation. A variety of preparative electrophoretic methodologies are briefly examined from the perspective of the methods used to establish fluid stability. Three instruments available at the Center for Separation Science, which have exceptionally large throughputs, are described and their performance evaluated.The recent technological advances in molecular biology have permitted the production of a variety of important molecules on a very large scale. In most cases the compounds of interest are produced in a broth with a large number of similar species and require purification. Compounds to be employed for therapeutic purposes require a high degree of purity. This is especially true if the molecule is the product of a transformed cell, as are monoclonal antibodies. The most common large scale purification techniques for proteins are chromatographic. Some of the limitations of these methods include resolution that suffers when scale-up is attempted, the need for more than one separation principle to accomplish a purification, and a batch rather than a continuous mode of operation.The most powerful methods for the analysis of protein mixtures are electrophoretic. Isoelectric focusing in polyacrylamide gels is capable of resolving proteins which differ in pi by 0.001 pH units (1). As many as ten thousand components can be resolved by two dimensional techniques (2). It is because of this power that analytical electrophoretic methods are used in numerous labs throughout the world. As a preparative methodology however, these techniques are

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