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. Author manuscript; available in PMC: 2020 Jul 21.
Published in final edited form as: J Mol Biol. 2017 Feb 21;429(7):1030–1044. doi: 10.1016/j.jmb.2017.02.010

Table 1.

Association and dissociation rates and affinities of actoxumab binding to purified TcdA and its fragments as determined by SPR

Toxin/Kd (pM)a,b fragment kon (M−1 s−1)a,b koff (sec−1)a,b
TcdA 1.87 × 105 ± 0.06 × 105 1.13 × 10−4 ± 0.13 × 10−4 610 ± 90
A1 5.92 × 105 ± 1.65 × 105 1.22 × 10−4 ± 2.01 × 10−4 220 ± 110
A4 3.19 × 105 ± 1.76 × 105 2.12 × 10−4 × 0.16 × 10−4 800 ± 490
TcdB Not measurable Not measurable Not measurable
a

The data presented are average ± standard deviation from two independent experiments.

b

koff = dissociation binding constant; kon = association binding constant; Kd = equilibrium dissociation constant.