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. 2013 Jan 10;288(9):6351–6362. doi: 10.1074/jbc.M112.431098

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 9. — Glycosylase activities of MBD4 and TDG. The glycosylase activity of the full-length MBD4 protein for mismatched, deamination, and/or oxidation products in the context of the ^5mCG/^5mCG sequence was assessed by NaOH cleavage of the resulting apyrimidinic site. We observed a significant digestion band for the strand containing either T or ^hmU in a mismatched wobble base. ^5mC, ^hmC, ^foC, and ^caC bases, each of which forms canonical Watson-Crick base pairs, were not removed by MBD4, whereas, human TDG exhibited activity toward ^foC and ^caC in addition to T and ^hmU bases.