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Nucleoside diphosphate (NDP) substrate binding was measured by competition with a fluorescent derivative of ADP, following the fluorescence anisotropy of the derivative.
Therefore, NO binding was measured by equilibrium titration of 5 µM Hb with NO solutions (7 µM to 2 mM).
The ANS (8-anilino-1-naphthalene-sulfonate) binding was measured by fluorescence emission with excitation at 380 nm and emission was recorded from 400 to 600 nm.
Lipid binding was measured by observing the change in the SPR angle as 150 µl of lipid analyte (various concentrations) in HBS-EP buffer flowed over the biosensor for 3 min at 50 µl/min.
For each antibody population, the specificity of the binding was measured by incubation with 100-fold excess of unlabeled GAD in homologous and heterologous inhibition assays, and the affinity of binding with GAD65 and GAD67 was measured in selected sera.
H4K5Ac binding was measured by ChIP-Seq assays.
Similar(40)
The binding is measured by the location of the so-called Fermi level of electrons in the metal; the higher the level, the lower is the binding.
Protein binding is measured by comparative fluorescence, providing a high throughput enzyme-linked immunosorbent assay [ 63].
The dose response curves for NP43-CGG, CGG, Cy34-SAv, and unconjugated SAv for specific binding were measured by averaging signal between 10 and 20 s at the end of each analyte injection, as very slow unbinding was observed.
The kinetics of ATP binding were measured by stopped-flow fluorescence in order to assess the range of rates over which Rho-MatB is suitable for real-time measurements.
In addition, Smad3 on DNA binding ability was measured by DNA immunoprecipitation using biotinylated Smad binding element DNA probes.
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