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Fig. 6 | Malaria Journal

Fig. 6

From: Strain-transcending neutralization of malaria parasite by antibodies against Plasmodium falciparum enolase

Fig. 6

Determination of association-dissociation rate constants for interaction between rPfeno and mAb H12E1. Thermodynamic and kinetic parameters for rPfeno-H12E1 interaction were measured using Surface Plasmon Resonance. a Sensogram shown represents 1:1 binding of bivalent mAb with dimeric enolase. Measurements were made in duplicates with different traces representing various concentrations of mAb (0.78–100 nM) used with fixed concentration of rPfeno on the CM5 chip. b Best fit kinetic parameters were derived from the sensogram. Dissociation constant KD was computed from association and dissociation rate constants. The half-life of mAb-Antigen complex was computed using t1/2 = (ln [0.5]/60*kd). Goodness of fit as judged by Chi2 was < 10% of Rmax

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