Figure 2. Purification and kinetic characterization of Plasmodium berghei M1 and M17 aminopeptidases, Pb-M1 and Pb-M17.

(A) Purification profile of PfA-M1 (black), Pv-M1 (red dash) and Pb-M1 (blue dash) and SDS–PAGE gel (inset) showing correct molecular mass and purity for each homolog. (B) Purification profile of PfA-M17 (black), Pv-M17 (red dash) and Pb-M17 (blue dash) and SDS–PAGE gel (inset) showing correct molecular mass and purity. (C) Pb-M1 activity profile in presence of increasing concentrations of divalent cations. Activity is highest in the absence of metal ions. (D) Pb-M17 activity in presence of increasing concentrations of divalent cations. Activity is highest in Co²⁺ and Mn²⁺ and increases as ion concentration increases. (E) Michaelis–Menten kinetics of Pb-M1. (F) Michaelis–Menten kinetics of Pb-M17. Assays carried out in biological triplicate and reported as mean ± standard error of the mean (SEM).