RAPID PURIFICATION AND BIOCHEMICAL CHARACTERISTICS OF LUMBROKINASE-III FROM EARTHWORM FOR USE AS A FIBRINOLYTIC AGENT

A fibrinolytic enzyme was purified from the earthworm (Lumbricus rubel lus) by column chromatography and identified as lumbrokinase type III. Affinity chromatography and NH2-terminal amino acid sequences indicat ed that this lumbrokinase III-2 (34.2 kDa) had additional amino acids at the carboxyl terminus of lumbrokinase III-1 (34 kDa). The lumbrokin ase III-1 was considerably stable at pH 2 to 11 and at up to 65 degree s C. It had trypsin-like characteristics with high substrate specifici ty against fibrin, suitable as a fibrinolytic agent. Degradation profi les of fibrinogen by lumbrokinase III-1 and their peptide sequences we re also investigated.