Figure 8: Characterization of recombinant proteins binding to PLG. In (a),(b), and (c) PLG (10 μg/mL) was immobilized in 96-well ELISA plates, and each recombinant protein at 0 to 1,000 nM was added for interaction. The binding was detected using antiserum raised in mice against each protein at appropriate dilutions (1 : 4,000 for LipL32; 1 : 5,000 for rLIC12238, LipL40, and MPL36; 1 : 1,000 for Lp29, Lp49, Lsa20, and rLIC11030; 1 : 500 for rLIC12730, Lsa66, and Lp30; 1 : 750 for rLIC11834 and rLIC12253), followed byhorseradish peroxidase-conjugated anti-mouse IgG. Data represent the mean absorbance values ± the standard deviation of six replicates for each experimental group. The results are representative of two independent experiments. In (d) The dissociation constant ( 𝐾 D ) was calculated based on ELISA data for the recombinant proteins that reached equilibrium up to a concentration of 1,000 nM.