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  • Title: Poly-D-lysine dependent inactivation of tissue plasminogen activator by a class PAI-2 inhibitor (minactivin).
    Author: Leung KC, Byatt JA, Stephens RW.
    Journal: Thromb Res; 1987 Jun 15; 46(6):767-77. PubMed ID: 3114909.
    Abstract:
    Two-chain tissue plasminogen activator (t-PA) was found to be inactive in a coupled colorimetric assay for plasminogen activators, but a high level of activity was obtained in the presence of poly-D-lysine. This stimulated activity was strongly inhibited by minactivin, a urokinase inhibitor, but unstimulated enzyme could be shown to be unaffected by minactivin. In the presence of poly-D-lysine minactivin was a very successful competitive inhibitor of t-PA with respect to the substrate, plasminogen. The Ki for minactivin determined by the Henderson method was 2.5 X 10(-12) M, compared to the Km for plasminogen determined as 0.6 X 10(-6) M. The value of Ki for minactivin with u-PA, determined under the same conditions, was 1.6 X 10(-11) M.
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