American Society of Hematology

Figure 3

$Figure 3. Influence of the mutations on MCP binding. Kinetic analyses were performed by SPR with recombinant soluble MCP on the chip. The running buffer was composed of 10 mM HEPES (pH 7.4), 0.005% Tween-20, and 25 mM NaCl. The recombinant C3 proteins were injected for 300 seconds at 30 μL/min, followed by dissociation of 300 seconds. The chip was regenerated by injection of 0.5 M NaCl. The results are presented as a fraction of WT binding. (A) Association rate constants for MCP binding. (B) Dissociation rate constants for MCP binding. (C) Affinity for MCP binding. (D) Example of SPR sensorograms and kinetic fits for MCP binding. (E) Model of the putative MCP binding site, obtained by molecular modeling and based on the structures of FH CCP1-48 and MCP.14 MCP CCP1-4 are indicated in cyan. Mutations are mapped in red. *P < .05; **P < .005, t test.$

Influence of the mutations on MCP binding. Kinetic analyses were performed by SPR with recombinant soluble MCP on the chip. The running buffer was composed of 10 mM 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 MCP binding. (B) Dissociation rate constants for MCP binding. (C) Affinity for MCP binding. (D) Example of SPR sensorograms and kinetic fits for MCP binding. (E) Model of the putative MCP binding site, obtained by molecular modeling and based on the structures of FH CCP1-4⁸ and MCP.¹⁴ MCP CCP1-4 are indicated in cyan. Mutations are mapped in red. *P < .05; **P < .005, t test.

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