Factor VIII:c concentrate virus inactivated: progress in purification by using classic chromatographic methods
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Updated: Nov 7, 2026

Detection and Removal of Nuclease Contamination During Purification of Recombinant Prototype Foamy Virus Integrase
Published on: December 8, 2017
Abstract:
This study was carried out with the aim of developing a production process for the manufacture of a highly purified factor VIII concentrate which is virus inactivated by pasteurization in liquid phase. Beside standard plasma protein separation techniques, the procedure uses a chromatographic step on anion exchanger, whose selectivity is increased by using high, but not destabilizing salt concentrations. The final product before stabilization has a specific activity higher than 300 IU/mg of protein, namely the highest specific activity reported for human factor VIII concentrates purified without the use of immunoadsorbents.

