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. 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.
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
D001779:Blood Coagulation Factors; D007704:Kininogens; D011480:Protease Inhibitors; C025667:prothrombin complex concentrates; D006493:Heparin; D003165:Complement System Proteins