Searched for: subject:"Protein%5C%2BBinding"
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Mulder, M. (author), Kohnert, U. (author), Fischer, S. (author), van Hinsbergh, V.W.M. (author), Verheijen, J.H. (author), Gaubius Instituut TNO (author)
The Escherichia coli-expressed recombinant plasminogen activator (r-PA) comprising the kringle 2 and protease domains of human tissue-type plasminogen activator (t-PA) has a four-fold longer half-life time in the circulation than t-PA, possibly resulting in an increased opportunity for r-PA to interact with the endothelial lining. In the present...
article 1997
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Bakker, A.H.F. (author), Weening-Verhoeff, E.J.D. (author), Verheijen, J.H. (author), Gaubius Instituut TNO (author)
To describe the role of the lysyl binding site in the interaction of tissue-type plasminogen activator (t-PA, FGK1K2P) with a forming fibrin clot, we performed binding experiments with domain deletion mutants GK1K2P, K2P, and the corresponding point mutants lacking the lysyl binding site in the absence and the presence of ε-amino caproic acid ...
article 1995
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Kluft, C. (author), Jie, A.F.H. (author), Sprengers, E.D. (author), Verheijen, J.H. (author), Gaubius Instituut TNO (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