A human factor VIIa concentrate and its effects in the hemophilic A dog.

Properties of a new concentrate of FVII/FVIIa, obtained by adsorption onto an inorganic adsorbent followed by a chromatographic step onto Q-Sepharose using a by-product of routine fractionation as starting material, are described. This fraction contains only small amounts of the other components of the prothrombin complex but it is enriched in Proteins C and S. This preparation is essentially free of FVIIICag.

Appraisal of the protein composition of prothrombin complex concentrates of different origins.

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.

Studies on prothrombin complex concentrates contact factors, complement components and proteinase inhibitors.

The behaviour of contact factors, complement components and antiproteases during the preparation of prothrombin complex concentrates by adsorption of the clotting components on DEAE-Sephadex has been studied. The pro-enzymes: factors XII, XI and prekallikrein were removed by pre-elution in function of the salt concentration. In contrast, high molecular weight kininogen was considerably enriched in PCC preparations.

Some proteins not belonging to the clotting or to the kallikrein-kinin system altered by kallikrein.

Plasma kallikrein activation occurs frequently during blood drawing and subsequent plasma handling. The purified enzyme was incubated with ceruloplasmin, inter-alpha-trypsin inhibitor and complement factor C4. Proteolysis caused by this enzyme was compared with the degradative effects of plasmin and thrombin.