Skip to main content
. 2006 Aug;141(4):1544–1554. doi: 10.1104/pp.106.084079

Figure 4.

Figure 4.

A, Time course of arsenate reductase activity, estimated as nmol NADPH oxidized; control (squares) complete assay mix with GRX2 but no reductase (squares), Arath;CDC25 (diamonds), P. vittata PvACR2 (circles), and yeast ScACR2 (triangles) in the presence of 40 mm arsenate in the assay mix. Data represents the mean (n = 3) ± se. B, Arsenate reductase activity measured as arsenite production over 45 min using LC-ICP-MS, with control (complete assay mix without enzyme), recombinant Arath;CDC25 (black), PvACR2 (gray), and ScACR2 (white) in the presence of 40 mm arsenate in the assay mix; nd, Not detected. Data represents the mean (n = 3) ± se. C, Phosphatase activity measured as hydrolysis of p-nitrophenol phosphate by Arath;CDC25, PvACR2, and ScACR2 recombinant protein. Data represents the mean (n = 3) ± se. D, Arsenate reductase activity (loss NADPH) with increasing concentrations of recombinant PvACR, at 40 mm arsenate in the assay mix. Data represents the mean (n = 3) ± se. E, Arsenate reductase activity of recombinant PvACR with increasing concentrations of arsenate in the assay mix. Data represents the mean (n = 3) ± se. Kinetic constants (±sd) determined using a nonlinear regression to the data, using the Marquardt-Levenberg algorithm.