Figure 3.

Kinetic analysis of inhibition of L1 RT by NRTIs. The L1 RT activity was measured as described in materials and methods. (A) Double reciprocal plot of the velocity of the L1 RT activity as a function of [32P]-dTTP substrate concentration. Increasing concentrations of substrate in the absence (diamond) or presence of 2 nM (square), 5 nM (triangle), 10 nM (circle) or 15 nM (+) AZTTP. (B) Double reciprocal plot of the velocity of the L1 RT activity as a function of [32P] dTTP substrate concentration. Increasing concentrations of substrate in the absence (diamond) or presence of 0.1 nM (square), 0.2 nM (triangle), 0.5 nM (circle) or 1 nM (+) d4TTP. (C) Double reciprocal plot of the velocity of the L1 RT activity as a function of [32P] dCTP substrate concentration. Increasing concentrations of substrate in the absence (diamond) or presence of 0.5 nM (square), 1 nM (triangle), 2 nM (circle) or 5 nM (+) ddCTP. (D) Double reciprocal plot of the velocity of the L1 RT activity as a function of [32P] dTTP substrate concentration. Increasing concentrations of substrate in the absence (diamond) or presence of 5 nM (square), 10 nM (triangle), 20 nM (circle) or 50 nM (+) 3TCTP.

Dai et al. BMC Biochemistry 2011 12:18   doi:10.1186/1471-2091-12-18
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