Journal of Experimental Medicine, Vol 146, 1033-1040, Copyright © 1977 by Rockefeller University Press
Plasmin inhibitor interactions. The effectiveness of alpha2-plasmin inhibitor in the presence of alpha2-macroglobulin
PC Harpel
alpha2-Plasmin inhibitor and alpha2-macroglobulin were allowed to compete
for the protease plasmin. The binding of the enzyme to these inhibitors was
assessed by two different but comparable methods. The interactions were
completed in 10 s of incubation, and transfer of plasmin from one inhibitor
to the other did not occur. Almost as much plasmin was bound to
alpha2-plasmin inhibitor in mixtures containing a large molar excess of
alpha2-macroglobulin relative to plasmin or alpha2-plasmin inhibitor, as
was bound in mixtures not containing alpha2-macroblobulin. These studies
demonstrate directly the effectiveness of alpha2-plasmin inhibitor in
binding and inhibiting plasmin in the presence of alpha2-macroglobulin, and
suggest that the alpha2-plasmin inhibitor may be the major circulating
plasmin inhibitor.
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