Two Human Immunochemically Distinct low Molecular Fibrinolytic Inhibitors

Recently a fast reacting α₂-antiplasmin (Müllertz 1972, Collen et al 1975) not identical with the inhibitor of the plasminogen activation (Hedner and Collen 1976) was described. Using the antiserum of Dr Aoki his inhibitor (Moroi and Aoki 19 76) was found to be identical with the α₂-antiplasmin but distinct from the inhibitor of the plasminogen activation. Furthermore the inter-α-anti-plasmin described by Gallimore (1975) was found to contain both material reacting with the antiserum of Collen and with the antiserum against the inhibitor of the plasminogen activation. By means of specific immunoadsorption of the fraction eluted close to the plasminogen activation inhibitor by the method described 1973 (Hedner 1973) these two inhibitors have been separated into two fractions, which do not cross react immunochemically. In a caseinolytic system plasma from which the α₂-antiplasmin was removed still has got an inhibitory activity against plasminogen activation. Also the α₂-antiplasmin, plasminogen, activation inhibitors as well as α₂-macroglobulin did not show any covariation in patients with different diagnoses. The inhibitor of the plasminogen activation did not interact with purified urokinase or plasmin but the α₂-antiplasmin forms complexes both with human and porcine plasmin.

Thus there seem to exist at least two different low molecular fibrinolytic inhibitors migrating as α₂-globulins in human blood.

 

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