LARGE-SCALE GEL-FILTRATION CHROMATOGRAPHY FOR THE PRODUCTION OF A SOLVENT DETERGENT-TREATED HIGH-PURITY FACTOR-VIII CONCENTRATE

Abstract. To produce a tri(n‐butyl)phosphate/sodium‐cholate‐treated intermediate‐purity factor VIII (FVIII) concentrate with a specific activity of about 1 IU/mg, we used a simple gel filtration step with Sephadex G25 to remove the solvent/detergent reagents from the final product. By exchanging the Sephadex G25 gel for a new high‐resolution gel (Sephacryl S400 HR), we obtained a high‐purity FVIII concentrate, by simultaneous elimination of about 98% of the extraneous proteins and removal of the solvent/detergent reagents, without reducing the FVIII:c yield and without altering the production scheme. With different protein analysis techniques we analysed the resulting FVIII concentrate and, comparing it to the formerly produced intermediate‐purity FVIII concentrate, demonstrated improved purity. © 1990 S. Karger AG, Basel