Abstract
AbstractAn experimental and theoretical investigation of the mechanism of electrophoretic elution is described. The rate of elution of bovine serum albumin from monoclonal antibody immunoadsorbents was observed to increase with increasing electric field, increasing fractional saturation, and decreasing height of the immunoadsorbent column. Slower elution rates were observed from immunoadsorbents possessing higher affinities and capacities. A reaction‐migration mechanism is proposed in which the packed bed is modeled as a continuous hydrogel and in which the electrical field causes antigen that has spontaneously dissociated to migrate through the column under conditions of bound‐free equilibrium. Good qualitative and quantitative agreement is obtained between experiment and the predictions of a numerical model. A membrane device suitable for large‐scale application of this technique is discussed.
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