[Analysis of the component constitution and substrate specificity of a fibrinolytic preparation from the fungus Flammulina velutipes].

The degree of heterogeneity of the proteolytic complex from the fungus Flammulina velutipes was studied by gel chromatography and analytical isoelectrofocusing. The fibrinolytic, thrombolytic, caseinolytic, endo- and aminopeptidase activities of the enzyme complex were compared to those of Aspergillus terricola and Streptomyces griseus proteinases. The proteolytic complex under study consists of at least two proteinases with pI 6.1 and 7.1, which possess fibrinolytic, thrombolytic and endopeptidase activities and of two aminopeptidases with pI 5.5 and 6.05. All these activities are inhibited by metal-chelating reagents. A low caseinolytic activity of the complex suggests that it can successfully be employed as a therapeutic agent.