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Research Article

Inhibition of purified bovine liver glutathione reductase with some metal ions

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Pages 68-73 | Received 03 Dec 2008, Accepted 01 Apr 2009, Published online: 29 Oct 2009

Figures & data

Figure 1. Inhibition of bovine liver GR by cadmium, nickel, and zinc ions.

Figure 1.  Inhibition of bovine liver GR by cadmium, nickel, and zinc ions.

Figure 2. Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Cd2+ (0–0.25 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), ×0.1 mM Cd2+, ○ 0.125 mM Cd2+, ◊ 0.15 mM Cd2+, + 0.25 mM Cd2+.

Figure 2.  Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Cd2+ (0–0.25 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), ×0.1 mM Cd2+, ○ 0.125 mM Cd2+, ◊ 0.15 mM Cd2+, + 0.25 mM Cd2+.

Figure 3. Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Cd2+ (0–0.25 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), ×0.1 mM Cd2+, ○ 0.125 mM Cd2+, ◊ 0.15 mM Cd2+, + 0.25 mM Cd2+.

Figure 3.  Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Cd2+ (0–0.25 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), ×0.1 mM Cd2+, ○ 0.125 mM Cd2+, ◊ 0.15 mM Cd2+, + 0.25 mM Cd2+.

Table 1. Mechanism of inhibition of bovine liver GR by metal ions and Ki values.

Figure 4. Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Ni2+ (0–0.6 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), ×0.1 mM Ni2+, ○ 0.2 mM Ni2+, ◊ 0.4 mM Ni2+, + 0.6 mM Ni2+.

Figure 4.  Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Ni2+ (0–0.6 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), ×0.1 mM Ni2+, ○ 0.2 mM Ni2+, ◊ 0.4 mM Ni2+, + 0.6 mM Ni2+.

Figure 5. Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Ni2+ (0–0.6 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), × 0.1 mM Ni2+, ○ 0.2 mM Ni2+, ◊ 0.4 mM Ni2+, + 0.6 mM Ni2+.

Figure 5.  Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Ni2+ (0–0.6 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), × 0.1 mM Ni2+, ○ 0.2 mM Ni2+, ◊ 0.4 mM Ni2+, + 0.6 mM Ni2+.

Figure 6. Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Zn2+ (0.1–0.4 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), × 0.1 mM Zn2+, ○ 0.2 mM Zn2+, ◊ 0.3 mM Zn2+, + 0.4 mM Zn2+.

Figure 6.  Lineweaver–Burk double reciprocal plot of initial velocity against GSSG as varied substrate and Zn2+ (0.1–0.4 mM) as inhibitor at fixed NADPH (0.1 mM) concentration. ▵ 0.1 mM NADPH (constant), × 0.1 mM Zn2+, ○ 0.2 mM Zn2+, ◊ 0.3 mM Zn2+, + 0.4 mM Zn2+.

Figure 7. Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Zn2+ (0.1–0.4 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), × 0.1 mM Zn2+, ○ 0.2 mM Zn2+, ◊ 0.3 mM Zn2+, + 0.4 mM Zn2+.

Figure 7.  Lineweaver–Burk double reciprocal plot of initial velocity against NADPH as varied substrate and Zn2+ (0.1–0.4 mM) as inhibitor at fixed GSSG (0.7 mM) concentration. ▵ 0.7 mM GSSG (constant), × 0.1 mM Zn2+, ○ 0.2 mM Zn2+, ◊ 0.3 mM Zn2+, + 0.4 mM Zn2+.

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