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KMID : 0379120050330020069
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Korean Journal of Mycology
2005 Volume.33 No. 2 p.69 ~ p.74
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Purification and Characterization of Fibrinolytic Enzyme from Lepista nuda
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Kim Jun-Ho
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Abstract
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Fibrinolytic enzyme has been isolated and purified from the edible mushroom, Lepista nuda. The apparent molecular mass of purified enzyme was estimated to be 34 KDa by SDS-polyacrylamide gel electrophoresis. 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. It has a pH optimum at $7.0.{\sim}9.5$, suggesting that the purified enzyme is an alkaline protease. It shows the maximum fibrinolytic activity at $55^{\circ}C$. The fibrinolytic activity was inhibited by phenylmethylsulfonyl fluoride, indicating that the purified enzyme is a serine protease. The activity of the purified enzyme was totally inhibited by $Hg^{2+}$.
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KEYWORD
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Fibrin plate assay, Fibrinolytic enzyme, Lepista nuda
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