Searched for: subject:"Protein%5C%2BBinding"
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de Man, F.H.A.F. (author), de Beer, F. (author), van der Laarse, A. (author), Smelt, A.H.M. (author), Havekes, L.M. (author), Gaubius Instituut TNO (author)
An in vitro assay to study lipolysis of very low density lipoproteins (VLDL) by heparan sulfate proteoglycan (HSPG-bound lipoprotein lipase (LPL) was developed. Optimal conditions for VLDL lipolysis by HSPG-bound LPL were obtained by incubating plastic wells with 0.5 μg HSPG and 1.5 μg LPL, subsequently. Control experiments with heparinase...
article 1997
Mulder, M. (author), Lombardi, P. (author), Jansen, H. (author), van Berkel, T.J.C. (author), Frants, R.R. (author), Havekes, L.M. (author), Gaubius Instituut TNO (author)
It has previously been shown that lipoprotein lipase (LPL) enhances the binding of low density lipoproteins (LDL) and very low density lipoproteins (VLDL) to HepG2 cells and fibroblasts, up to 80-fold. This increase in binding is LDL receptor-independent and is due to a bridging of LPL between extracellular heparan sulfate proteoglycans (HSPG)...
article 1993
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