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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-02

AUTHORS

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

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. More... »

PAGES

169-172

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1005384625974

DOI

http://dx.doi.org/10.1023/a:1005384625974

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002961393


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