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The protein contaminants of prothrombin complex preparations obtained by adsorption onto ion exchangers and namely DEAE-Sephadex were studied.  Among them a high amount of C4 accompanied by some C4- binding protein was noticed. Certain preparations contain as much as 20 times the normal plasma concentration of C4. This complement component is able to form an anaphylatoxin. Its molecular integrity has been checked by immunoelectrophoresis and rocked electrophoresis. Its degradation by several enzymes is shown.  The clotting component concentrates contain also high amounts of kininogen. The enrichment of high molecular weight (H.M.W.) kininogen is comparable to the one observed for C4. Its presence was assessed with an antiserum specific for this protein and the ability of the kininogen to supply kinin was checked on guinea pig ileon.  The potential thrombogenicity of prothrombin complex preparations has been attributed to contact factors. It is shown in this study that factor XII and its derivatives as well as PK can be easily removed during the processing of the fraction. However, kininogen displays the same affinity for the ion exchanger than the clotting components.

Presence Of Complement Factor C4 And HMW Kininogen In Prothrombin Complex Concentrates