Figure 4

Biochemical characterization of Mt-DsbA. A. Mt-DsbA does not facilitate correct disulfide bond formation and folding of denatured hirudin, whereas Mt-DsbF and Ec-DsbA do. B. Mt-DsbA does not possess insulin reductase activity as observed for Mt-DsbE and Mt-DsbF. In contrast, Ec-DsbC possesses disulfide reductase activity, and Ec-DsbA has reduced reductase activity in comparison to Ec-DsbC. C. In vitro Dsb protein isomerase activity was assessed by using the scrambled RNaseA (scRNaseA) refolding assay. Mt-DsbA has disulfide bond isomerase activity in contrast to Mt-DsbE and Mt-DsbF, which do not possess the ability to refold scRNaseA. The fraction of native RNaseA activity were calculated and plotted against incubation time.