American Society of Hematology

Figure 2

$Figure 2. Influence of the mutations on FH binding. Kinetic analyses were performed by SPR with immobilized FH or FH CCP19-20. The running buffer was composed of 10 mM N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid (HEPES; pH 7.4), 0.005% Tween-20, and 25 mM NaCl. The recombinant C3 proteins were injected for 300 seconds at 30 μL/min, followed by dissociation of 300 seconds. The chip was regenerated by injection of 0.5 M NaCl. The results are presented as a fraction of WT binding. (A) Association rate constants for FH binding. (B) Dissociation rate constants for FH binding. (C) Affinity for FH binding. (D) Example of SPR sensorograms and kinetic fits for FH binding. (E) Affinity for FH CCP19-20 binding. The black arrows represent mutant proteins for which the binding was low and kinetic constants could not be calculated. *P < .05; **P < .005, t test.$

Influence of the mutations on FH binding. Kinetic analyses were performed by SPR with immobilized FH or FH CCP19-20. The running buffer was composed of 10 mM N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid (HEPES; pH 7.4), 0.005% Tween-20, and 25 mM NaCl. The recombinant C3 proteins were injected for 300 seconds at 30 μL/min, followed by dissociation of 300 seconds. The chip was regenerated by injection of 0.5 M NaCl. The results are presented as a fraction of WT binding. (A) Association rate constants for FH binding. (B) Dissociation rate constants for FH binding. (C) Affinity for FH binding. (D) Example of SPR sensorograms and kinetic fits for FH binding. (E) Affinity for FH CCP19-20 binding. The black arrows represent mutant proteins for which the binding was low and kinetic constants could not be calculated. *P < .05; **P < .005, t test.

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