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Figure 1

From: Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone

Figure 1

Structural analysis of the recombinant Oryza sativa ascorbate peroxidase 2 (OsAPX2) protein. The purified OsAPX2 protein was identified using 12% sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions (a) and 10% native-PAGE (b). (c) Size exclusion chromatography (SEC) analysis of purified OsAPX2. The separated proteins were collected in four fractions (F1–F4) for further analysis. The values in the chromatogram represent the molecular weights of the protein standards: blue dextran (>2000 kDa), thyroglobulin (669 kDa), ferritin (440 kDa), aldolase (158 kDa), ovalbumin (44 kDa) and carbonic anhydrase (29 kDa). Structural analysis of the OsAPX2 protein fractions (inset). Each fraction corresponds to a peak from SEC (F1–F4) and these were analysed using 10% native-PAGE (upper panel) or 12% SDS-PAGE (lower panel).

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