Table 1

Increase in binding of plasminogen and tPA to fibrin on limited proteolysis by plasmin is impaired in the presence of polyP

ControlpolyP65 (325μM)
Plasminogen 3.9 ± 0.13 2.6 ± 0.11* 
tPA 3.1 ± 0.09 2.2 ± 0.13 
ControlpolyP65 (325μM)
Plasminogen 3.9 ± 0.13 2.6 ± 0.11* 
tPA 3.1 ± 0.09 2.2 ± 0.13 

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.

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