Purification, characterization and crystallization of a group of earthworm fibrinolytic enzymes from Eisenia fetida.
Seven fibrinolytic enzymes were purified from the earthworm Eisenia fetida. The molecular weights of the enzymes were 24663, 29516, 29690, 24201, 24170, 23028 and 29595, and the respective isoelectric points were 3.46, 3.5, 3.5, 3.68, 3.62, 3.94 and 3.46. All the proteases showed different fibrinolytic activity on fibrin plates. Studies on substrate specificity and inhibition indicated that they belonged to different types of serine proteases. N-Terminal sequencing indicated their high homology to those from the earthworm Lumbricus rubellus. All the enzymes have been crystallized.
Wang
Feng
F
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China.
Wang
Chao
C
Li
Mei
M
Gui
Lulu
L
Zhang
Jiping
J
Chang
Wenrui
W
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization / Q000379:methods; D004791:Enzyme Inhibitors; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009835:Oligochaeta / Q000737:chemistry*; D010958:Plasminogen / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D005343:Fibrinolytic Agents; D010958:Plasminogen; D012697:Serine Endopeptidases