Searched for: subject:"Protein%5C%2BBinding"
(1 - 3 of 3)
document
Rijken, D.C. (author), Barrett-Bergshoeff, M.M. (author), Jie, A.F.H. (author), Criscuoli, M. (author), Sakharov, D.V. (author), Gaubius Instituut TNO (author)
Amediplase (K2tu-PA) is a hybrid plasminogen activator, consisting of the kringle 2 domain of alteplase and the protease domain of urokinase. The objective of this study was to determine the in vitro clot penetration of amediplase in relation to its fibrin binding and to compare the properties with those of alteplase. The clot lysis activity of...
article 2004
document
Rijken, D.C. (author), Jie, A.F.H. (author), Gaubius Laboratory TNO Preventie en Gezondheid (author)
Reteplase is a protein consisting of the kringle-2 and protease domains of tissue-type plasminogen activator (t-PA). Because intravenous heparin will be used as an adjunct to thrombolytic therapy with reteplase, we investigated the interactions in vitro between heparin and reteplase as well as between heparin and recombinant t-PA (alteplase) as...
article 1996
document
Gaubius Instituut TNO (author), Kluft, C. (author), Jie, A.F.H. (author), Sprengers, E.D. (author), Verheijen, J.H. (author)
Inhibition of tissue-type plasminogen activator (t-PA) by pooled plasma could be ascribed for only 60% to the endothelial cell type PA inhibitor. The residual inhibition is ascribed to a so-far undescribed plasma component present at 0.2 nmol/l. This component shows reversible binding to t-PA with an apparent K(i) of 10 pmol/l (does not hinder t...
article 1985