Abstract

PRIME technology is a novel preparative electrophoretic isolation method for the purification of biological proteins based on molecular size and charge. Molecular charge, generated by the choice of a suitable buffered pH system, is employed in combination with polyacrylamide hydrogel membranes of selected porosities to separate molecules. By using both size and charge as restrictive factors for purification, the PRIME method is able to isolate molecules with high yield and purity. In this paper, we discuss the use of PRIME technology in the purification of plasma proteins. In the present work, albumin at 93% purity was purified at high yield (98%). Using albumin-depleted plasma for further processing of immunoglobulins (IVIG), we were able to obtain an IVIG product yield as high as 92% and purity as high as 88%. Since PRIME does not use solvents or require sub-zero temperatures and is well-suited for plasma purification from modest plasma volumes, we propose the application of PRIME as a cost-effective and safe alternative to Cohn fractionation.

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