Purification, characterization and crystallization of a group of earthworm fibrinolytic enzymes from Eisenia fetida

被引：51
|
作者：
Wang, F [1 ]
Wang, C [1 ]
Li, M [1 ]
Gui, LL [1 ]
Zhang, JP [1 ]
Chang, WR [1 ]
机构：
[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源：
BIOTECHNOLOGY LETTERS | 2003年 / 25卷 / 13期
关键词：
crystallization; earthworm fibrinolytic enzyme; purification; substrate specificity;
D O I：
10.1023/A:1024196232252
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Seven fibrinolytic enzymes were purified from the earthworm Eisenia fetida. The molecular weights of the enzymes were 24 663, 29 516, 29 690, 24 201, 24 170, 23 028 and 29 595, 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.
引用
收藏
页码：1105 / 1109
页数：5
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