title: Studies on prothrombin complex concentrates contact factors, complement components and proteinase inhibitors.
abstract: 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. C4 of the complement system displayed an analogous behaviour. C1s reached a 4-5 fold plasma concentration but C3 only 30% of the normal plasma level. The prothrombin complex concentrate contained no antithrombin III nor alpha 2M nor alpha 2 antiplasmin but a three fold plasma concentration of C1-inactivator and a 15 fold increase of inter-alpha-trypsin inhibitor. NAPTT (Non Activated Partial Thromboplastin Time) ratios did not seem to be in accordance with either the presence or the absence of contact enzymes. Moreover 0.20 M NaCl appeared as the minimal pre-elution molarity necessary to ensure a NAPTT ratio above thrombogenic values. Molecular alteration of high molecular weight kininogen and C4 was observed and its significance discussed. Complex formation between C1-inactivator and proteases was shown to be another sign of undesirable proteolytic events.
mesh_terms: D001779:Blood Coagulation Factors / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D003165:Complement System Proteins / Q000302:isolation & purification; D006493:Heparin; D006801:Humans; D007704:Kininogens / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000302:isolation & purification
chemical_list: D001779:Blood Coagulation Factors; D007704:Kininogens; D011480:Protease Inhibitors; C025667:prothrombin complex concentrates; D006493:Heparin; D003165:Complement System Proteins