Activation of human plasminogen in the presence of rPDHA-C and degradation of fibrinogen.

<p>(A) Plasminogen bound to rPDHB is converted into plasmin. Wells of ELISA plates were coated with rPDHA-D and incubated with plasminogen. Urokinase (uPA) and plasmin-specific substrate (D-Val-Leu-Lys-<i>p</i>-nitroanilide dihydrochloride; S) were added and incubated overnight. The activity of plasmin was detected by measuring the absorbance at 405 nm. BSA acted as control. Means and standard deviations of eight parallels (** = P<0.01; student’s t-test). (B) Human fibrinogen is degraded by rPDHB. Recombinant protein rPDHB and BSA as control were immobilized in wells of ELISA plates and incubated with plasminogen. After washing, uPa and fibrinogen were added. Samples were taken at different time points up to 2 hours. Degradation products were determined using goat anti-fibrinogen and polyclonal peroxidase-conjugated anti-goat IgG. Data represent means and standard deviations of eight parallels (* = P<0.05; student’s t-test).