Biomedical Science Letters (대한의생명과학회지)
- Volume 12 Issue 3
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- Pages.225-231
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- 2006
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- 1738-3226(pISSN)
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- 2288-7415(eISSN)
Characterization of a Fibrinolytic Serine Protease from a Wild Mushroom, Lepista nuda
Abstract
Fibrinolytic enzyme was purified from the fruiting bodies of Lepista nuda, using DEAE-Cellulose chromatography, Phenyl Sepharose chromatography, and Mono-S column chromatography. The substance has a molecular weight of 30006.62 Da as measured by MALD-TOF mass spectrometry. The N-terminal amino acid sequence of the enzyme was Tyr-Pro-Ser-Pro-Ser-His-Gln-Thr-Ala-Val-Asn-Ala-Ile-Ile-X. The activity of the enzyme was inhibited by PMSF, indicating that the enzyme is a serine protease. No inhibition was found with E-64, pepstatin, and EDTA. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to