mAb | Kda | koffb (×10−4) (1/s) | pH50 | % Bound at pH 8c |
---|---|---|---|---|
nM | ||||
A1 WT | 65 | 39.5 | 6.39 | 29 |
A1 V308P | 1.5 | 2.0 | 6.87 | 25 |
A1 T250Q/M428L | 2.7 | 2.7 | 6.64 | 17 |
B1 WT | 195 | 141 | 6.25 | 46 |
B1 V308P | 0.5 | 1.0 | 6.77 | 19 |
B1 T250Q/M428L | 1.7 | 1.9 | 6.77 | 22 |
C1 WT | 66 | 52.5 | 6.22 | 41 |
C1 V308P | 0.6 | 1.0 | 6.52 | 12 |
C1 T250Q/M428L | 4.7 | 4.3 | 6.41 | 8 |
D1 WT | 91 | 5.5 | 6.36 | 45 |
D1 V308P | 0.5 | 1.0 | 7.10 | 28 |
D1 T250Q/M428L | 8.5 | 8.9 | 6.73 | 18 |
E1 WT | 160 | 176 | 6.39 | 66 |
E1 V308P | 1.4 | 3.0 | 6.71 | 20 |
E1 T250Q/M428L | 13.4 | 1.5 | 6.67 | 25 |
↵a Kd (koff/kon · 1 × 109); data determined from SPR kinetic analyses at pH 6.0. No direct binding of FcRn to the IgGs was observed at pH 7.4 in SPR experiments at FcRn concentrations as high as 5 μM.
↵b Determined from SPR kinetic analyses at pH 6.0.
↵c Percentage of the total antibody in preformed complexes that remained FcRn-bound at pH 8 as determined by ELISA.