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. 2020 Aug 3;9(3):37. doi: 10.3390/antib9030037

Table 3.

Affinity of anti-V mAbs to the Y. pestis V-antigen determined by Biacore SPR.

mAb a KD (nM) ± SE ka × 104 (1/Ms) ± SE kd × 10−4 (1/s) ± SE
10.1 24.3 ± 0.9 b 5.67 ± 0.42 13.8 ± 1.05
84.1a 10.7 ± 0.5 b,c 9.11 ± 0.35 9.66 ± 0.2
84.1b 25.4 ± 1.5 b,c 7.73 ± 0.33 19.3 ± 0.43
7.3 4.03 ± 0.27 16.9 ± 0.47 6.98 ± 0.56
141.1a 2.46 ± 0.06 b,c 22.8 ± 0.49 5.64 ± 0.10
141.1b 0.77 ± 0.06 b,c 40.1 ± 0.51 3.07 ± 0.19

a mAb 74.1 was not functional in the kinetic analysis of binding to the V-antigen (Figure S4). b Difference in KD relative to 7.3 is p < 0.0001. c There was a significant difference between the KD of unbiotinylated and biotinylated mAbs (p < 0.0001).