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 immunoabsorbents.