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. 2010 May 28;38(19):6785–6795. doi: 10.1093/nar/gkq433

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), 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. — Dependence of product formation on concentration of ATP and GTP competitors. (A) Time course of self-thio-phosphorylation reactions at 1 mM ATPγS (ribozyme K8) or GTPγS (ribozyme K37) in the presence of ATP or GTP competitors at various concentrations. (B) Observed rate constants (k_obs, in units of min⁻¹) and calculated plateau values (f_max) obtained by fitting the experimental data to a first-order exponential equation. Each data point is the average of at least three independent assays.