Abstract

Column ion exchange chromatographic processes were developed for the production of immune serum globulin (ISG) for intravenous use. Sequential chromatography on two cross-linked agarose gel anion exchangers yielded the same immunoelectrophoretic pure ISG as a single column DEAE-Sephadex procedure with the advantage of repeated 'in column' cycling. ISG with a low content of aggregated IgG and low anticomplementary activity was prepared from plasma with 53-69% efficiency. The ISG prepared by these processes was characterized with respect to the content of IgA, prekallikrein activator (PKA), plasminogen, fragmentation, and heavy chain subclass distribution.

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