Dimerization of polymorphic S326C OGG1

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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 (lanes 1 and 2) and S326C OGG1 (lanes 3 and 4) at a concentration of 5 µM were incubated with 1 mM of BM[PEO] cross-linker in the absence (lanes 1 and 3) or presence (lanes 2 and 4) of 10 µM duplex 8-oxoG·C substrate. Lane M, molecular weight marker. Reactions were analyzed by SDS–PAGE on 4–20% acrylamide gels. () Wild-type OGG1 (2.5 µM) in lanes 1–4 was incubated with 1 mM BM[PEO] in the presence of 0 (lane 1), 1.25 µM (lane 2), 2.5 µM (lane 3) and 5 µM (lane 4) S326C OGG1.