Two fibrinolytic enzymes from the autolysate of Lumbricus rubellus were purified in homogeneous form. Their molecular sizes were 31,000 (Enz1) and 35,000 (Enz2) Da. respectively. However, the N-Terminal amino acid sequences of Enz1 and Enz2 were exactly the same: Ile-Val-Gly-Gly-Ile-Glu-Ala-Arg-Pro-Tyr-Glu-Phe-Pro-Trp-Gln-. These results indicate that Enz1 is a shortened form of Enz2 formed during autolysis. When a synthetic substrate, Ile-Pro-Arg-pNA, was used, the catalytic activity were observed in the pH range of 5-10 and the kinetic parameters including $K_m$ (1.6 ${mu}m$) and $V_{max}$ (40 nmol/jmin/mg) were almost identical between the two enzymes. However, the fibrinolytic activity of Enz2 was at least 1.25 times higher than that of Enz1, suggesting that the C-terminal region of Enz2 is important in fibrinolysis but not in amidolysis. Furtheimore. fibrinolytic activity of the enzymes was increased by the addition of the lipid extracted from L. rubellus in the presence of $MgCl_2$ or $CaCl_2$. The stimulatary effect of lipid on Enz2 was higher compared to Enz1.