The protein composition of 12 different prothrombin complex concentrates, including 2 purified factor
IX concentrates and 2 activated fractions, was evaluated. There is a clear difference between ion exchanger-prepared
fractions and those obtained by adsorption onto calcium phosphate. The former contain high molecular weight
kininogen and complement components, the latter only trace amounts of these proteins but relatively high quantities
of the pro- and even partially activated enzymes of the contact phase. Calcium phosphate adsorbed preparations
contain less VIII : CAg than the DEAE-Sephadex-prepared fractions. The inorganic adsorbent showed higher affinity
for IgG than the ion exchangers.