A Method Development Study of the Production of Albumin from Animal Blood by Ion-Exchange Chromatography

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Abstract
The conditions of operation of ion-exchange Chromatography are examined for the production of albumin from bovine serum and plasma. The ion-exchanger is a Vistec-DEAE cellulose. Of the various modes of chromatographic operation available, the most suitable for proteins is shown to be adsorption onto the whole column followed by stepwise elution. The method is developed by studying; experimentally, the effect of major parameters so as to point the way to optimization. Prior dialysis and dilution of the feed are beneficial. Other conclusions apply to the large-scale separation of proteins in general. In particular, column length, eluent velocity, feed band width, and packing rigidity are parameters where trade-offs will be needed to maximize performance. If suitable precautions are taken in column design, scale-up can be achieved by increasing the column diameter alone. Albumin separated chromatographically is superior in electrophoretic purity to that produced by the commercial Cohn precipitation method.

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