Purification of recombinant human basic fibroblast growth factor: stability of selective sorbents under cleaning in place conditions.

Human basic fibroblast growth factor (bFGF) was produced from recombinant Escherichia coli by high-cell-density cultivation. In order to develop a purification strategy for large-scale purification, chromatographic sorbents with different anionic functional groups were compared in terms of selectivity for bFGF and stability under cleaning in place (CIP) conditions. Heparin-Sepharose CL-6B, Fractogel EMD-SO3- 650 (S) and SP-Sepharose (high performance) were found suitable for this purpose with decreasing selectivity in that order.