A recombinant chimeric plasminogen activator (dscu-PA(B)) was constructed, consisting of the decorsin (platelet aggregation inhibitor), fused via a 15-amino-acid linker (Gly₄Ser)₃ sequence to the N-terminal of the B chain of urokinase (comprising Leu159 through Leu 411). The recombinant protein was produced in E.coli host strain Rosetta(DE3)plysS after IPTG induction and exited in inclusion body. The stability of plasmid was studied. After refolded in vitro, the chimeric protein was purified by Zinc chelate-Sepharose chromatography and SP Sepharose chromatography in sequence. The molecular weight was 33.735kD by MALDI-TOF analysis. The special activity of the chimera was 90000IU/mg detected by fibrin plate determination. It was also shown that chimera inhibited ADP-induced platelet aggregation in a concentration dependent manner. Inhibition of approximately 50% aggregation was achieved at a concentration of approximate 0.31μmol/L, which was a little lower inhibition potential than that of decorsin. These results showed that the chimeric protein had not only high thrombolytic activity but also anti-thrombus function. Further evaluation of the thrombolytic potential in appropriate animal models seems to be investigated.