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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].
Similar(58)
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.
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.
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.
H4K5Ac binding was measured by ChIP-Seq assays.
Nucleotide binding was measured by the filtration method.
Similarly, Colo205 cells were cultured with 2F-Fuc and CTB binding was measured by flow cytometry.
Non-specific binding was measured by immersing sensors without CaM in analyte and was negligible in all cases.
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