Аннотация:The micromycete Aspergillus tabacinus was described as the first microorganism producing an extracellular protease with protein Clike activity. It was also shown thatthe enzymes secreted by this producer demonstrated fibrinogenolytic activity. This property may be useful for the development of a drug with not only anticoagulant butalso thrombolytic activity. For the subsequent development of a therapeutic agent it is important to establish whether protein Clike and fibrinogenolytic activities aremanifested by one enzyme or are characteristic of different secreted proteins of the micromycete. Fractional salting out of proteins from the culture fluid resulted in sixdifferent fractions and revealed several enzymes with target proteolytic activities. Desalting of all protein samples was performed using gelfiltration. Spectrophotometricanalysis showed the presence of high amidolytic activity towards chromogenic peptide substrates of activated protein C, urokinase, and plasmin in all six proteinsamples. Zymography revealed several enzymes with fibrinogenolytic and fibrinolytic activities in different protein samples including 2 highly active low molecular weightproteins (≈12 and 18 kDa). The obtained data suggest that protein Clike and fibrinogenolytic activities are characteristic of different enzymes of A. tabacinus, since itwas previously shown that protein Clike, urokinaselike and plasminlike activities can be exhibited by a protease with a molecular weight of about 30 kDa but lowmolecular proteases with such activities were not found. Further search for a method for the combined isolation of target enzymes from the culture fluid of themicromycete or the production of desired proteins in heterologous expression systems will allow the development of a pharmaceutical preparation that simultaneouslyexhibits anticoagulant and fibrinolytic activities.