4.3 Article

Isolation, purification, and resolution of the extracellular proteinase complex of Aspergillus ochraceus 513 with fibrinolytic and anticoagulant activities

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MICROBIOLOGY
卷 70, 期 5, 页码 519-522

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MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1023/A:1012343718772

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extracellular proteinases; protein C activator; affinity chromatography; column chromatography

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The extracellular proteinase complex of the microscopic fungus Aspergillus ochraceus 513 was isolated, purified, and resolved by affinity chromatography on bacillichin-silochrom and subsequent column chromatography on DEAE-Toyopearl 650M. The extracellular enzyme of the protein C activator type had a molecular mass of 36.5 kDa and activity close to that of the Agkistrodon snake venom protein C activator. The fibrinolytic and anticoagulant activities of the enzyme were investigated.

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