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. 2010 Mar 25;38(13):4313–4324. doi: 10.1093/nar/gkq187

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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 6. — Soluble DNMT1 is more sensitive to degradation that chromatin bound DNMT1. (A) upper panel, western blot of HCT116 cells treated with the indicated doses of 5-aza-dC for 12 h. Whole cell proteins were fractionated by differential solubility in PBS/0.5% Triton X-100. The soluble fractions (S) fractions were separated from the chromatin bound insoluble (INS) fractions by centrifugation. In the lower panel the effects of pre-treatment of the cells with MG132 are shown. GAPDH and Histone H4 serve as a loading controls for the soluble fraction and insoluble fractions respectively, and serve to verify that chromatin was separated as expected. (B) Pre-treatment with MG132 reduces the DNA hypomethylating effects of 5-aza-dC.