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. 2022 Mar 3;298(4):101798. doi: 10.1016/j.jbc.2022.101798

Table 2.

Fc binding kinetics to human FcγRIIIa

pH Fc variant FcγRIIIa V158
kon ± SD
(×105 M–1s–1)
koff
(×10–2 s–1)
Kd ± SD
(nM)
Kd,SS
(nM)
Chi2Kd,SS
(nm2)
pH 6.5 Wild-type 4.5 ± 1.1 4.6 ± 1.2 102 ± 2.4 103 0.0303
Acid-Fc 5.7 ± 1.3 7.4 ± 1.1 131 ± 9.9 115 0.0300
pH 7.4 Wild-type 4.9 ± 1.7 6.4 ± 1.9 134 ± 11.3 139 0.0384
Acid-Fc 5.1 ± 1.9 11 ± 1.9 236 ± 47 225 0.0297
pH Fc variant FcγRIIIa F158
kon ± SD
(×105 M–1s–1)
koff
(×10–2 s–1)
Kd ± SD
(nM)
Kd,SS
(nM)
Chi2Kd,SS
(nm2)
pH 6.5 Wild-type 3.0 ± 3.2 11.9 ± 1.1 401 ± 74 418 0.0356
Acid-Fc 3.4 ± 6.7 17.7 ± 0.5 538 ± 107 603 0.0298
pH 7.4 Wild-type 2.8 ± 1.9 13.4 ± 2.3 484 ± 96 513 0.0445
Acid-Fc 2.5 ± 4.2 22.6 ± 2.2 909 ± 154 1089 0.0347

The association constant(kon), dissociation constant (koff), and equilibrium dissociation constant (Kd = koff/kon) as well as the steady-state dissociation constant (Kd,SS) were determined for hu4D5 antibodies with human IgG1 Fc or acid-Fc and measured by BLI. Mean values and SD (n = 4) are shown, except for Kd,SS values for which the Chi2 values from the fit are shown.