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Specific binding experiments revealed that RvD1 binds with high affinity (Kd = 0.2 nM) to human neutrophils.
Characterization analysis and binding experiments revealed that mag-MFMIP beads had outstanding magnetic property, large adsorption capacity and high competitive selectivity to most of the commonly seen environmental estrogens.
The binding experiments revealed that the on-rate and off-rate constants in the first ligand-occupation reaction increased with increasing the ligand density, which resulted in stable values of the dissociation constant.
Competitive binding experiments revealed that MRS1334 blocked the binding of CA200645 with a K i value of 9.0±0.1 nM (n=4; Fig 1D).
As kinetic binding experiments revealed that approximate equilibrium was reached after a 3 h incubation period with scFv (6 C and D), the incubation time for binding studies was adjusted to this incubation time.
Our subsequent binding experiments revealed that DV1 and SDF-1α, as well as the well-known small molecule ligands of CXCR4, AMD3100 and IT1t, all inhibited the binding of FITC-DV1 to CXCR4 in our assay (IC50 values listed in Table S2 of the Supporting Information), suggesting that the site of binding of FITC-DV1 to CXCR4 overlaps with those of SDF-1α, 12G5 Ab, AMD3100, and IT1t.
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DA transporter binding experiment revealed that the three MPTP-intoxicated groups had a similar severe nigrostriatal fiber denervation of the striatum (Fig. 1D) as shown in other occasions with the very same MPTP regimen [12].
The results of our ITC-binding experiments reveal that increasing the chain length of XOS promotes binding to TrCel7A.
The binding experiments revealed important sex differences in the density of SERT proteins.
Competition binding experiments revealed higher affinity of the phytoestrogens for ERss than for ER[alpha].
Ligand binding competition experiments revealed that the binding sites on hIgG for the two octapeptides were similar to those for Protein A. Finally, hIgG was purified from human serum with high purities and recovery yields with the two peptide affinity columns.
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