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. 2015 Jan 27;59(2):1052–1060. doi: 10.1128/AAC.04433-14

TABLE 2.

Association and dissociation rates and affinities of actoxumab and bezlotoxumab binding to purified toxins, as determined by surface plasmon resonance

Antibody/toxin Strain High-affinity binding site
Low-affinity binding site
kon (M−1 s−1)a koff (s−1) Kd (nM) kon (M−1 s−1) koff (s−1) Kd (nM)
Actoxumab/TcdA 087b 1.9 × 105 ± 0.1 × 105 1.1 × 10−4 ± 0.1 × 10−4 0.61 ± 0.09 NDc ND ND
027 1.7 × 104 ± 0.2 × 104 1.5 × 10−4 ± 0.2 × 10−4 8.7 ± 1.5 ND ND ND
078 5.0 × 104 ± 3.4 × 104 2.2 × 10−4 ± 1.0 × 10−4 5.2 ± 2.2 ND ND ND
Bezlotoxumab/TcdB 087 1.0 × 106 ± 0.1 × 106 5.2 × 10−5 ± 2.0 × 10−5 0.050 ± 0.014 4.8 × 106 ± 1.4 × 106 1.6 × 10−2 ± 0.8 × 10−2 3.9 ± 2.9
027 3.9 × 105 ± 0.8 × 105 2.8 × 10−4 ± 0.3 × 10−4 0.75 ± 0.16 ND ND ND
078 6.7 × 105 ± 0.3 × 105 4.4 × 10−4 ± 1.9 × 10−4 0.65 ± 0.27 ND ND ND
a

Values are means ± standard deviations of two separate determinations.

b

Strain 087 is VPI 10463.

c

ND, not determined because the data best fit a single-site model.