ACTIVATING EFFECT OF THE PLASMINOGEN ACTIVATORS ON PLASMINOGENS OF DIFFERENT MAMMALIA SPECIES

Plasmin (E.C. 3.4.21.7.) is a major serine proteolytic enzyme responsi ble for fibrinolytic function in mammalia blood plasma. It is formed b y activation of proenzyme plasminogen with the known activators such a s urokinase(UK, E.C. 3.4.21.31.), tissue-type plasminogen activator (t -PA, E.C. 3.4.21.67.) or streptokinase (SK) (1, 2). At the present tim e the plasminogen activators and the mechanisms of their activating ef fect on human plasminogen are rather completely investigated. However using different mammalia species for fibrinolytic process studied on v arious thrombus models in vivo sets a problem about efficiency of plas minogen activation with main activators in pure systems, containing pl asminogens of these animals. There is limited information concerning t he activation process peculiarities of these plasminogens (3-6). In th is communication we give the results of the experimental animal plasmi nogen activation rate investigation with t-PA, urokinase, streptokinas e and streptokinase-human plasminogen complex in model system of pure proteins.