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. Author manuscript; available in PMC: 2018 Nov 1.

Published in final edited form as: DNA Repair (Amst). 2017 Sep 1;59:1–8. doi: 10.1016/j.dnarep.2017.08.010

Fig. 3 — Single-turnover kinetic results for hOGG1 and UDG in NCP substrates. Kinetic time courses were performed to evaluate the activity of (A) hOGG1 or (B) UDG on either free duplex DNA (●) or NCP substrates with off-dyad lesions. The NCP substrates contained lesions of varying rotational position: OUT ( ), MID ( ), or IN ( ). Experiments were conducted using 20 nM NCP substrate and 0.64 µM glycosylase in 20 mM Tris-HCl (pH 7.6), 25 mM NaCl, 75 mM KCl, 1 mM EDTA, 1 mM DTT, 200 µg/ml BSA. Data for free duplex DNA substrates were fit to a single exponential equation; all NCP data were fit to a double exponential equation. Error bars represent the standard error (n=4).

Inline graphic — Single-turnover kinetic results for hOGG1 and UDG in NCP substrates. Kinetic time courses were performed to evaluate the activity of (A) hOGG1 or (B) UDG on either free duplex DNA (●) or NCP substrates with off-dyad lesions. The NCP substrates contained lesions of varying rotational position: OUT ( ), MID ( ), or IN ( ). Experiments were conducted using 20 nM NCP substrate and 0.64 µM glycosylase in 20 mM Tris-HCl (pH 7.6), 25 mM NaCl, 75 mM KCl, 1 mM EDTA, 1 mM DTT, 200 µg/ml BSA. Data for free duplex DNA substrates were fit to a single exponential equation; all NCP data were fit to a double exponential equation. Error bars represent the standard error (n=4).