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. Author manuscript; available in PMC: 2021 Oct 1.
Published in final edited form as: Biochim Biophys Acta Mol Cell Res. 2020 Jun 26;1867(10):118786. doi: 10.1016/j.bbamcr.2020.118786

Table 5. Equilibrium and kinetic constants for FGF14 self-interaction by SPR.

Kinetic constants were calculated based on data represented in Figure 5B. The KD represents the average between the kinetic KD, calculated using the simplest Langmuir 1:1 interaction model (KD=koff/kon), and the steady-state saturation (affinity) KD. Data are mean ± SD. Note that fitting kinetic data for the phosphorylated peptide was difficult due to kinetic constants approaching limits of instrument detection, and thus the estimated values should be interpreted only qualitatively.

KD (μM) kon (M−1 s−1) koff (s−1)
FGF14WT Peptide 1.01 ± 0.07 1.69×104 ± 8.1×102 4.64×10−2 ± 7.2×10−3
FGF14Y158-p Peptide 181.1 ± 109 3.29×102 ± 1.2×102 8.97×10−2 ± 3.9×10−2
FGF14Y158A Peptide 7.02 ± 0.21 2.32×104 ± 1.6×103 1.58×10−1 ± 7.6×10−3