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

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Abstract

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.

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Authors and Affiliations

  1. Chinese Academy of Sciences, National Laboratory of Biomacromolecules, Institute of Biophysics, Beijing, 100101, P.R. China

    Feng Wang, Chao Wang, Mei Li, Lulu Gui, Jiping Zhang & Wenrui Chang

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  1. Feng Wang
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  2. Chao Wang
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  3. Mei Li
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  4. Lulu Gui
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  5. Jiping Zhang
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  6. Wenrui Chang
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Correspondence to Wenrui Chang.

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Wang, F., Wang, C., Li, M. et al. Purification, characterization and crystallization of a group of earthworm fibrinolytic enzymes from Eisenia fetida . Biotechnology Letters 25, 1105–1109 (2003). https://doi.org/10.1023/A:1024196232252

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  • DOI: https://doi.org/10.1023/A:1024196232252

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