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Research Article

The inhibition kinetics of yeast glutathione reductase by some metal ions

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Pages 489-495 | Received 05 Oct 2006, Accepted 13 Nov 2006, Published online: 04 Oct 2008

Figures & data

Figure 1 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and ZnSO4 (0.05–1 mM) as inhibitor at a fixed NADPH (0.1 mM) concentration. *0.1 mM NADPH (constant); □ 0.05 mM ZnSO4 ;○ 0.1 mM ZnSO4; Δ 0.5 mM ZnSO4; ⋄1 mM ZnSO4.

Figure 1 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and ZnSO4 (0.05–1 mM) as inhibitor at a fixed NADPH (0.1 mM) concentration. *0.1 mM NADPH (constant); □ 0.05 mM ZnSO4 ;○ 0.1 mM ZnSO4; Δ 0.5 mM ZnSO4; ⋄1 mM ZnSO4.

Figure 2 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and ZnSO4 (0.05–1 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.05 mM ZnSO4;Δ 0.1 mM ZnSO4;*0.5 mM ZnSO4;○ 1 mM ZnSO4.

Figure 2 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and ZnSO4 (0.05–1 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.05 mM ZnSO4;Δ 0.1 mM ZnSO4;*0.5 mM ZnSO4;○ 1 mM ZnSO4.

Figure 3 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and CaCl2 (0.8–1.6 mM) as inhibitor at a fixed NADPH (0.1 mM) concentrations. *0.1 mM NADPH (constant); □ 0.8 mM CaCl2; ○ 1 mm CaCl2; Δ 1.2 mM CaCl2; ⋄1.6 mM CaCl2.

Figure 3 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and CaCl2 (0.8–1.6 mM) as inhibitor at a fixed NADPH (0.1 mM) concentrations. *0.1 mM NADPH (constant); □ 0.8 mM CaCl2; ○ 1 mm CaCl2; Δ 1.2 mM CaCl2; ⋄1.6 mM CaCl2.

Figure 4 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and CaCl2 (0.8–1.6 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.8 mM CaCl2; Δ 1 mm CaCl2; *1.2 mM CaCl2; ○ 1.6 mM CaCl2.

Figure 4 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and CaCl2 (0.8–1.6 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.8 mM CaCl2; Δ 1 mm CaCl2; *1.2 mM CaCl2; ○ 1.6 mM CaCl2.

Figure 5 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and NiSO4 (0.1–0.4 mM) as inhibitor at different fixed NADPH (0.1 mM) concentrations. *0.1 mM NADPH (constant); ○ 0.1 mM NiSO4; ▪ 0.2 mM NiSO4; Δ 0.3 mM NiSO4; ⋄ 0.4 mM NiSO4.

Figure 5 Lineweaver-Burk double reciprocal plot of initial velocity against GSSG as varied substrate and NiSO4 (0.1–0.4 mM) as inhibitor at different fixed NADPH (0.1 mM) concentrations. *0.1 mM NADPH (constant); ○ 0.1 mM NiSO4; ▪ 0.2 mM NiSO4; Δ 0.3 mM NiSO4; ⋄ 0.4 mM NiSO4.

Figure 6 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and NiSO4 (0.1–0.4 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.1 mM NiSO4; Δ 0.2 mM NiSO4; *0.3 mM NiSO4; ○ 0.4 mM NiSO4.

Figure 6 Lineweaver-Burk double reciprocal plot of initial velocity against NADPH as varied substrate and NiSO4 (0.1–0.4 mM) as inhibitor at different fixed GSSG (0.7 mM) concentrations. ⋄ 0.7 mM GSSG (constant); □ 0.1 mM NiSO4; Δ 0.2 mM NiSO4; *0.3 mM NiSO4; ○ 0.4 mM NiSO4.

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