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Kinetics of wild-type and S326C OGG1

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posted on 2011-12-30, 17:52 authored by Jeff W. Hill, Michele K. Evans

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Taken from "Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase"

Nucleic Acids Research 2006;34(5):1620-1632.

Published online 20 Mar 2006

PMCID:PMC1405821.

© The Author 2006. Published by Oxford University Press. All rights reserved

Wild-type and S326C OGG1 (2.5 nM) were incubated with increasing amounts (3.25–100 nM) of duplex 8-oxoguanine substrates having C (), T (), G () or A () opposite 8-oxoG, or with a substrate having an abasic site opposite C (). Glycosylase reactions with 8-oxoguanine paired with C, T and G, were incubated for 15 min at 37°C. AP-lyase reactions with the AP·C substrate and glycosylase reactions with 8-oxoG opposite A were incubated for 1 h at 37°C. Reactions were terminated and analyzed as described in Materials and Methods. Data points are means of three independent experiments with standard deviation.

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