Skip to main content
. 2001 Sep 11;98(20):11224–11229. doi: 10.1073/pnas.191282098

Figure 3.

Figure 3

(A–C) Reduction levels of Prx-QAt under the redox conditions were determined by AMS labeling. The purified Prx-QAt was in the oxidized form. A total of 3 μM of Prx-QAt was incubated with 50 μM CuCl2 or the indicated concentration of DTT in the absence (A) or presence of 4 μM (B) or 0.04 μM (C) Trx-m. Then the reduction level of Prx-QAt was determined by the incorporation of AMS and the change of the mobility during SDS/PAGE. (D) Trx-m dependent peroxidase activity of Prx-QAt was measured with H2O2 as a substrate and NADPH as a reductant. The decrease in the absorbance at 340 nm was monitored (trace e). In traces a–c, Trx-m, Trx reductase, or Prx-QAt was omitted from the reaction mixture, respectively. In trace d, Trx-mC41S was used instead of Trx-m.