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. 2009 Apr 16;37(11):3714–3722. doi: 10.1093/nar/gkp227

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© 2009 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. — Inhibition of the phosphohydrolase activity by nucleotide analogs. (A) The standard GTPase activity was performed in the presence of 20 μM [γ-^32P]GTP. The various nucleotide analogs were added at a single concentration of 100 μM and the inhibition of the GTPase activity was evaluated by monitoring the release of radiolabeled inorganic phosphate, which was separated from the GTP substrate by thin-layer chromatography. (B) Dose–response inhibition of the GTPase activity by A₁₂ (2′,3′-dideoxy-GTP). (C and D) Competitive inhibition of the GTPase reaction by A₁₂. The GTPase activity was evaluated in the absence (filled square) or presence of five (open square) or 10 μM (open circle) of A₁₂. (E) Dixon plot of the inhibition performed at each fixed concentration of GTP substrate, five (filled square), 10 (filled triangle), or 50 μM (open square).