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. 2013 Dec 11;42(5):3246–3260. doi: 10.1093/nar/gkt1281

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© The Author(s) 2013. 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/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — Bmt5 binds SAM in vitro. To demonstrate SAM binding of Bmt5, the heterologously expressed Bmt5 was purified to homogeneity by Ni-NTA and cation exchange chromatography and its binding was analyzed by iTC. The left panel display titration of SAM into the Bmt5 protein (sample cell). The upper panel shows the baseline-corrected titration data, and the lower panel shows the binding isotherm fit to a model for a single SAM binding site. The right panel shows different parameters calculated from the titration analysis. The heat signals obtained from iTC were analyzed using Origin software supplied by Micro Cal yielding the stoichiometry (N), the equilibrium association constant Ka as well as the enthalpy (ΔH) and the entropy (ΔS) of binding. Bmt5 binds SAM with a K_d of 109 ± 10.8 µM.