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. 2016 Nov 30;174(1):70–81. doi: 10.1111/bph.13654

Figure 3.

Figure 3

sMAdCAM‐binding assays – thermodynamic KD in buffer, KD in human serum, KD,app{100%serum}. (A) Binding interaction samples are paired as reference and test samples in control or binding samples with (B) resulting saturation binding isotherm used to quantify the thermodynamic KD of PF‐00547659 to rhMAdCAM.Fc fusion protein in PBS. Measuring the binding interaction of PF‐00547659 to endogenous sMAdCAM in 0.1% healthy human serum, (C) binding interaction samples are paired and (D) corresponding saturation binding isotherm used to quantify the thermodynamic KD. Measuring interactions with increasing human serum in 10, 25, 35 and 50% serum using the same (E) binding interaction samples are paired and (F) overlay of saturation binding isotherms of PF‐00547659 to serum sMAdCAM. (G) Plot of KD,app versus serum percentage to determine the KD,app{100%serum}. Error bars for all plots represent the standard deviations of replicate trials over five consecutive experiments performed on different days (n = 4–5).