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Demonstration of a fast-acting inhibitor of plasminogen activators in human
plasma
EK Kruithof, C Tran-Thang, A Ransijn and F Bachmann
This report describes a plasmatic, fast-acting, specific inhibitor
(antiactivator) of tissue-type plasminogen activator (t-PA) and urokinase
(UK). After addition of t-PA to human plasma, biexponential decay of
activity occurred. The initial rapid inhibition of t-PA activity (half-life
of approximately one minute) was correlated with the formation of a complex
of a molecular weight of 110,000, suggesting a molecular weight in the
order of 40,000 for the antiactivator. Diisopropylfluorophosphate
(DFP)-inactivated t-PA did not form complexes with antiactivator. The
second-order rate constant for the interaction of t-PA with antiactivator
is in the order of 10(7) mol/L-1 sec-1. In plasma, UK added at low
concentrations rapidly formed complexes of a mol wt of 95,000.
Preincubation of the plasma with t-PA prevented complex formation of UK,
and vice versa, suggesting that the same inhibitor inactivates both t-PA
and UK. After exhaustion of the antiactivator, t-PA and UK formed complexes
with alpha 2-antiplasmin and C1'-inhibitor at a low rate.
Volume 64,
Issue 4,
pp. 907-913,
10/01/1984
Copyright © 1984 by The American Society of Hematology
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