Searched for: subject:"Protein%5C%2BBinding"
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document
Nieuwenhuizen, W. (author), Voskuilen, M. (author), Hermans, J. (author), Gaubius instituut TNO (author)
The present study was undertaken as a step to delineate further the localization of the calcium-binding sites in fibrinogen and to assess the anticlotting properties of fibrinogen degradation products. To this purpose, fragments Y were prepared by plasmin digestion of human fibrinogen in the presence of added Ca2+, and purified. We found that,...
article 1982
document
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
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Gaubius instituut TNO (author), Havekes, L. (author), van Hinsbergh, V. (author), Kempen, H.J. (author), Emeis, J. (author)
The human hepatoma cell line Hep G2 was studied with respect to metabolism of human low-density lipoprotein (LDL). The Hep G2 cells bind, take up and degrade human LDL with a high-affinity saturable and with a low-affinity non-saturable component. The high-affinity binding possesses a K(D) of 25 nM-LDL and a maximal amount of binding of about 70...
article 1983