• Title/Summary/Keyword: Tricholoma sejunctum

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Purification and Characterization of Fibrinolytic Enzyme from Tricholoma sejunctum

  • Kim, Jun-Ho
    • Biomedical Science Letters
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    • v.8 no.4
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    • pp.245-250
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    • 2002
  • Fibrinolytic enzyme has been purified from the edible mushroom, Tricholoma sejunctum using DEAE-cellulose chromatography, Phenyl-Sepharose chromatography and Mono-S column chromatography. The apparent molecular mass of purified enzyme was estimated to be 17100 Da by SDS-polyacrylamide gel electrophoresis and 19000 Da by gel filtration, Indicating that it was a monomer. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. It has a pH optimum at pH 9.5, suggested that purified enzyme was a alkaline protease. The activity of purified enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that purified enzyme is a metalloprotease. The activity of purified enzyme was increased by Zn$^{2+}$ and Co$^{2+}$, however, the enzyme activity was totally inhibited by Hg$^{2+}$.

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Characterization of a Fibrinolytic Metalloenzyme from a Wild Mushroom, Tricholoma sejunctum (쓴송이버섯으로부터 분리한 혈전용해 금속효소의 특성 연구)

  • Kim, Jun-Ho;Cho, Seung-Koo
    • The Korean Journal of Mycology
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    • v.32 no.2
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    • pp.119-124
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    • 2004
  • Metalloenzyme was purified from the fruiting bodies of Tricholoma sejunctum. MALDI-TOF and ICP/MS analyses revealed that the enzyme had a molecular weight of 18788.25 and includes $Zn^{2+}$ ion. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. The activity of the enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme was a metalloprotease. No inhibition was found with E-64 and pepstatin. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to $40^{\circ}C$. The activity of the enzyme was increased by $Zn^{2+}$ and $Co^{2+}$, while it was totally inhibited by $Hg^{2+}$. The enzyme hydrolyzes $A{\alpha}$ subunit of human fibrinogen but did not show any reactivity for $B{\beta}$ and ${\gamma}$ form of human fibrinogen.

Screening Test of Wild Mushroom Extracts for Fibrinolytic Activity

  • Kim, Jun-Ho
    • Biomedical Science Letters
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    • v.8 no.3
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    • pp.173-177
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    • 2002
  • To investigate the fibrinolytic activities of the Korean basidiomycetes, the Extracts of 50 wild mushrooms were tested for their fibrinolytic activites. Extract from Tricholoma sejunctum showed 175% increased activity to that of plasmin 1.0 U/ml. Marasmius siccus showed 54% of activity, and Laetiporus sulphureus var. miniatus and Macrolepiota procera, 43% and 26% activities, respectively to that of plasmin. But, Cystoderma amianthinum, Lepiota sp., Coprinus sp., Lycoperdon sp. were less than 10% of plasmin activity.

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