Abstract
A fibrinolytic enzyme was purified from the earthworm (Lumbricus rubellus) by column chromatography and identified as lumbrokinase type III. Affinity chromatography and NH2-terminal amino acid sequences indicated that this lumbrokinase III-2 (34.2 kDa) had additional amino acids at the carboxyl terminus of lumbrokinase III-1 (34 kDa). The lumbrokinase III-1 was considerably stable at pH 2 to 11 and at up to 65°C. It had trypsin-like characteristics with high substrate specificity against fibrin, suitable as a fibrinolytic agent. Degradation profiles of fibrinogen by lumbrokinase III-1 and their peptide sequences were also investigated.
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Park, YD., Kim, JW., Min, BG. et al. Rapid purification and biochemical characteristics of lumbrokinase III from earthworm for use as a fibrinolytic agent. Biotechnology Letters 20, 169–172 (1998). https://doi.org/10.1023/A:1005384625974
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DOI: https://doi.org/10.1023/A:1005384625974