Table 1.
Binding affinities of recombinant rat, cynomolgus monkey, and human FcRn proteins to immobilized rhumAbs at pH 6.0.
| Mean KD ( ± SD) (μM) |
||
|---|---|---|
| Species of FcRn | rhumAb1 | rhumAb2 |
| Rat | 2.0 ± 0.1 | 1.2 ± 0.02 |
| Cynomolgus monkey | 3.0 ± 0.1 | 2.7 ± 0.1 |
| Human | 3.5 ± 0.2 | 3.2 ± 0.2 |
KD = dissociation equilibrium constant.
Notes: Mean and standard deviation (SD) were calculated based on 3 independent experimental runs. The binding data of rat FcRn to immobilized rhumAbs were obtained by kinetics analysis using a monovalent binding model in the Biacore T200 evaluation software. The averaged ka and kd values for rhumAb1 are (2.1 ± 0.2)×104 1/Ms, and (4.2 ± 0.2)×10−2 1/s; for rhumAb2 are (3.8 ± 0.1)×104 1/Ms, and (4.4 ± 0.1)×10−2 1/s. The binding data of cynomolgus monkey and human FcRn proteins to immobilized rhumAbs were obtained by steady-state equilibrium analysis using Biacore T200 evaluation software.