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EJNMMI Research
Fig. 5 | EJNMMI Research

Fig. 5

From: New approaches for the reliable in vitro assessment of binding affinity based on high-resolution real-time data acquisition of radioligand-receptor binding kinetics

Fig. 5

Comparison of obtained and reported K i values. Inhibitory constants of the A3R antagonists MRS1191, MRS1523 and FE@SUPPY, respectively, were obtained from competitive real-time cell-binding studies at ambient temperature with 0.7 nM [125I]-AB-MECA on CHO-K1-hA3R cells (group A) and compared to the corresponding K i values obtained from traditional binding assays, as previously reported in the literature (group B). Differences for MRS1191, MRS1523 and FE@SUPPY among groups are statistically not significant (ns = P > 0.05), using ordinary two-way ANOVA with Sidak’s correction. Data in the graph are shown as mean ± SEM from three independent experiments (see Table 1 for summary of dedicated K i values)

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