A Fibrinolytic Metalloprotease from the Fruiting Bodies of an Edible Mushroom, Armillariella mellea

概要

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A fibrinolytic metalloprotease has been purified from the fruiting bodies of the edible honey mushroom (Armillariella mellea). The enzyme has a molecular weight of 18538.1508,as measured by MALDI-TOF mass spectrometry and includes Zn^<2+> ion as found by ICP/MS. The N-terminal amino acid sequence, XXYNGXTXSRQTTLV, do not match any known protein or open reading frame. It hydrolyzes fibrinogen as well as fibrin, but does not show any proteolytic activity for other blood proteins such as thrombin, human albumin, bovine albumin, human IgG, hemoglobin, or urokinase. This protease hydrolyzes both Aα and Bβ subunits of human fibrinogen with equal efficiency. The enzyme activity was strongly inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme is a metalloprotease. No inhibition was found with PMSF, E-64,pepstatin, and 2-mercaptoethanol. The activity of the purified enzyme was slightly increased by Mg^<2+>, Zn^<2+>, and Co^<2+>, but the enzyme was totally inhibited by Hg^<2+>. It has broad substrate specificity for synthetic peptides, and a pH optimum at 7,suggested that the purified enzyme was a neutral protease. It was thermally stable up to 60℃ and the maximum fibrinolytic activity was at 55℃.
社団法人日本農芸化学会の論文
1999-12-23