PREPARATIVE PURIFICATION OF RECOMBINANT THROMBOLYTIC PROTEIN FROM COMPLEX BIOLOGICAL MIXTURES

The purification of recombinant thrombolytic protein from a crude fermentation broth mixture was examined in antibody exchange (ABx) chromatographic system. ABx system was shown to exhibit unique selectivity for the recombinant protein broth mixture and higher total binding capacity for the recombinant protein than cation-exchange system. The research with the ABx system indicated that these mixed mode interaction systems could be successfully employed in the displacement mode using DEAE-dextran as the displacer.