Isolation and some characterizations of a glycosylated fibrinolytic enzyme of earthworm, Eisenia fetida.

Resin coupled with m-aminophenylbornic acid was used to isolate a glycosylated component from homogenate of earthworm (Eisenia fetida). The fraction showed a single band on SDS-PAGE with a molecular weight of 34, 193 Da determined by mass spectroscopy. The N-terminal region is AQVCCPDI, different from those of earthworm fibrinolytic enzymes reported previously (Nakajima et al. 1993). This glycosylated component showed an activity on digesting both Chromozym-TH and fibrin, suggesting that it is a novel fibrinolytic enzyme.