Figure 2

Enzymatic activity analysis of the recombinant OsAPX2 protein. (a) The APX activity of purified OsAPX2 protein. The concentrations of purified OsAPX2 used were: 0.25 mM (○), 0.5 µM (▼), 0.75 µM (Δ), 1 µM (■) and 0 µM (●) OsAPX2 protein. (b) Molecular chaperone activity of purified OsAPX2 protein. The molecular chaperone activity of OsAPX2 protein was measured using malate dehydrogenase (MDH) as a substrate. Thermal aggregation of MDH was induced at 43 °C for 15 min. The control plot (●) shows the thermal aggregation of MDH in the absence of OsAPX2. The molecular chaperone activity of OsAPX2 was evaluated at 1:0.5 (○), 1:1 (▼), 1:2 (Δ), and 1:4 (■) molar ratios MDH:OsAPX2. The data are expressed as means of at least three independent experiments.