@article{ref1,
title="A cyclopeptidic suicide substrate preferentially inactivates urokinase-type plasminogen activator",
journal="Biochemical and biophysical research communications",
year="1991",
author="Reboud-Ravaux, M. and Vilain, A. C. and Boggetto, N. and Maillard, J. and Favreau, C. and Xie, J. and Mazaleyrat, J. P. and Wakselman, M.",
volume="178",
number="1",
pages="352-359",
abstract="c[Arg-aB-(CH2+SCH3 phi)-Gly4] was designed and studied as a mechanism-based inactivator (suicide substrate) for plasminogen activators (u-PA and t-PA) and plasmin. This compound inhibited u-PA and fulfills criteria expected for the involvement of an enzyme-activated inhibitor: first-order and irreversible process, saturation kinetics, protection by substrate. The limiting first-order rate constant kinact and the apparent enzyme-inhibitor dissociation constant KI were 0.021 s-1 and 9 microM, respectively at pH 7.5 and 25 degrees C. The activation of plasminogen by u-PA is compromised after this enzyme has been treated by the reagent. Plasmin and t-PA were inactivated 40- and 2330-fold less efficiently than u-PA, respectively.<p /><p>Language: en</p>",
language="en",
issn="0006-291X",
doi="10.1016/0006-291x(91)91821-s",
url="http://dx.doi.org/10.1016/0006-291x(91)91821-s"
}