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.
Li
Li
L
Lab of Visual Information Processing, Center for Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang Dist, 15 Da-Tun Rd, Beijing 100101, China.
Zhao
Jing
J
He
Rong-Qiao
RQ
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D009835:Oligochaeta / Q000201:enzymology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D004798:Enzymes; D005343:Fibrinolytic Agents; D006023:Glycoproteins