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Biotechnology Letters

, Volume 20, Issue 2, pp 169–172 | Cite as

Rapid purification and biochemical characteristics of lumbrokinase III from earthworm for use as a fibrinolytic agent

  • Yong-Doo Park
  • Jong-Won Kim
  • Byong-Goo Min
  • Jeong-Won Seo
  • Jong-Moon Jeong
Article

Abstract

A fibrinolytic enzyme was purified from the earthworm (Lumbricus rubellus) by column chromatography and identified as lumbrokinase type III. Affinity chromatography and NH2-terminal amino acid sequences indicated that this lumbrokinase III-2 (34.2 kDa) had additional amino acids at the carboxyl terminus of lumbrokinase III-1 (34 kDa). The lumbrokinase III-1 was considerably stable at pH 2 to 11 and at up to 65°C. It had trypsin-like characteristics with high substrate specificity against fibrin, suitable as a fibrinolytic agent. Degradation profiles of fibrinogen by lumbrokinase III-1 and their peptide sequences were also investigated.

Keywords

Enzyme Peptide Carboxyl Column Chromatography Fibrinogen 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Chapman and Hall 1998

Authors and Affiliations

  • Yong-Doo Park
    • 1
  • Jong-Won Kim
    • 1
  • Byong-Goo Min
    • 1
  • Jeong-Won Seo
    • 2
  • Jong-Moon Jeong
    • 2
  1. 1.Department of Biomedical Engineering, College of MedicineSeoul National UniversitySeoulSouth Korea
  2. 2.Department of Life Science, College of Natural SciencesThe University of SuwonHwasung-Gun Kyonggi-DoKorea

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