Summary
Human factor IXa was purified 5,000-fold from serum by ion exchange chromatography. The preparation
was free from other clotting factors. Both pH sensitivity and heat stability of purified
factor IXa appeared to be different from those of factor IX in the plasma. The molecular weight
of human factor IXa is 80,000 as estimated from gel-filtration experiments. Modification of seryl or
histidyl side chains abolished the activity of factor IXa.