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Binding experiments were also attempted using isothermal titration calorimetry, however, again we encountered problems with low signal and high noise.
Binding experiments were also performed on HCT 116 cells and on human umbilical vein endothelial cells (HUVEC) at various cell densities.
To investigate the influence of GSL clustering on VLP binding, experiments were also performed under experimental conditions where GalCer is in the fluid phase.
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The pUC19 fragment used in the binding experiments was also tested but the exchange was very inefficient, probably due to the much higher affinity of H1 for chromatin than for the pUC19.
Therefore, iron binding and releasing experiments were also performed to determine the bioactivity of the rhLF purified from the milk of the marker-free transgenic cows.
To investigate the specificity of binding to PSMA, experiments were also carried out in the presence of 10 μM PMPA, a known high-affinity PSMA inhibitor (1.4 nM, [7]).
Both binding and activation experiments were also performed with the Tir phosphorylation mimicking Y474D mutant of Tir (data not shown).
These experiments were also the first demonstration of in vitro binding of heavy metal cations to CusA.
Experiments were also carried out as before to assess the PrP binding capacity of mte after exposure to the metals.
Batch equilibrium experiments were also performed for both PHA and PFA to investigate Pb-DOM binding in the absence of soil.
Binding experiments were carried out with a Monolith NT.115 Series instrument (Nano Temper Technologies GMBH).
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