TABLE 2.
Albumin speciesa | FcRn species | FcRn variant | ka | kd | KD | KD Reqb |
---|---|---|---|---|---|---|
103/Ms | 10−3/s | μm | μm | |||
MSAc | Mouse | WT | 4.2 ± 0.5 | 39.4 ± 3.1 | 9.3 ± 0.4 | NDd |
MSAc | Human | WT | 3.8 ± 0.0 | 3.1 ± 0.1 | 0.8 ± 0.2 | ND |
HSAb | Mouse | WT | NAe | NA | NA | 86.2 ± 4.1 |
HSAf | Human | WT | 2.7 ± 1.3 | 12.2 ± 5.9 | 4.5 ± 0.1 | 4.6 ± 0.5 |
HSAb | Mouse | L166R/G167E | NA | NA | NA | 26.8 ± 0.1 |
MSAc | Human | R164L/E165G | 0.7 ± 0.1 | 3.4 ± 0.1 | 4.8 ± 0.1 | ND |
MSAc | Mouse | L166R/G167E | 2.7 ± 0.2 | 18.5 ± 0.5 | 6.8 ± 1.8 | ND |
HSAc | Human | R164L/E165G | 3.2 ± 0.1 | 26.3 ± 0.2 | 8.2 ± 0.1 | ND |
b The steady-state affinity constant was obtained using an equilibrium (Req) binding model supplied by the BIAevaluation 4.1 software. The kinetic values represent the average of triplicates.
c The kinetic rate constants were obtained using a simple first-order (1:1) bimolecular interaction model.
d ND, not determined.
e NA, not acquired because of fast kinetics.
f The kinetic values have been published in Ref. 10.