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. 2007 Oct 16;35(20):6973–6983. doi: 10.1093/nar/gkm695

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© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Determination of the K_d for AZT-TP in competition with TTP. (A) Exonuclease-deficient holoenzyme (100 nM) was preincubated with 90 nM 25/45-mer DNA (radiolabeled primer) and then rapidly mixed with Mg²⁺, 1 μM TTP and various concentrations of AZT-TP [0 (open circle), 50 (filled circle), 200 (open square) and 400 (filled square) μM]. Each data set was fitted using a single exponential equation to obtain the observed rate of incorporation. (B) The observed rates were plotted as a function of AZT-TP concentration and fitted using Equation (3) to obtain an apparent K_d of 53 ± 13 μM for AZT-TP binding, a Y-intercept of 9.7 ± 0.3 s⁻¹, and an overall decrease in the observed rate of 8.6 ± 0.6 s⁻¹. According to Equation (4), a true K_d of 20 ± 7 μM for AZT-TP in competition with TTP can be defined.