Summary
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. Cls 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 α2M nor α2 antiplasmin but a three fold plasma concentration of Cl-inactivator and a
15 fold increase of inter-α- 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.
Key words
Prothrombin complex - Contact factors - Complement components - Proteinase inhibitors
