Increase in binding of plasminogen and tPA to fibrin on limited proteolysis by plasmin is impaired in the presence of polyP
Binding of plasminogen and tissue plasminogen activator (tPA) to fibrin surfaces formed with or without polyP65 was analyzed before and after partial lysis with plasmin. The mean fold-increase in binding ± SEM is calculated after degradation of the fibrin surface with plasmin from 4 concentrations of plasminogen (125, 250, 500, 1000nM) and tPA (31.25, 62.5, 125, 250nM).
P < .001 when comparing control with polyP65 values.
P < .005 when comparing control with polyP65 values.