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. 2015 Jan 6;43(2):1069–1080. doi: 10.1093/nar/gku1328

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Recombinant RHA is a highly active helicase. (A) Eluted RHA fractions from the Hi-Trap nickel column stained with Coomassie Blue. (B) Heparin column-purified RHA stained with Coomassie. (C) One nanomolar RHA separated 1-nM dsRNA in a temperature- and time-dependent fashion to single strands. (D) The initial rates of the reactions were plotted against the temperatures. The linear correlation coefficient of this plot was found as r² = 0.9251. All reactions were carried out three times. (E) Michaelis–Menten kinetics graph, the x-axis represents the substrate (dsRNA) concentration in nM, and the y-axis represents the initial velocity at the corresponding substrate concentration. The kinetics experiments were repeated three times and differences among individual results represented in the error bars. Inset of (E): Lineweaver–Burk transformation plot of the RHA helicase enzyme reaction.