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Highly purified α2M, plasmin /PL/ and urokinase/UK/ preparations of human origin and synthetic chromogenic peptide substrates H-D-Val-Leu-Lys-pNA /S-225l/,  L/ and SBTI but decreased gradually in the presence of aprotinin depending upon the concentration of the latter and also with time. In contrast to PL, streptokinase-PL complex was inhibited by α2M only very slightly if at all. Heparin-free preparations of HMW /54,000/ and LMW /33 000/ of UK /Choay/ were found to have Km values of 7.81 × 10-5 and 7.14 × l0-5mole/l respectively /S-2444, 0.1M Tris-HCl pH 8.0 containing 0.05M NaCl,37°/. When calculated per mole their activities on S-2444 were almost identical. Although both types of UK formed complexes with α2M, completion of the reaction took 12-24 hrs. The rate of reaction with HMW was about double that of LMW. The results indicate that α2M does not play a significant role as an inhibitor of plasminogen activation. Its only important role in the inhibition of the fibrinolytic system appears to be its function as an overflow inhibitor of plasmin remaining after α2APL inhibition.

Role Of α2-Macroglobulin /α2M/ In The Inhibition Of The Fibrinolytic System