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. 2003 Apr;185(7):2203–2209. doi: 10.1128/JB.185.7.2203-2209.2003

FIG. 1.

FIG. 1.

Different binding properties of wild-type and mutant OxyR to unmethylated agn43 regulatory region. Results obtained from EMSA with cell extracts containing OxyR are shown in panel A (lanes 2 to 5), with OxyR(H198R) in panel B, and with OxyR(A233V) in panel C. Amounts of total protein added were 0 μg (lanes 1 and 6), 0.42 μg (lanes 2), 0.85 μg (lanes 3), 2.55 μg (lanes 4), and 4.25 μg (lanes 5). Also shown is the shift obtained with 7 ng of purified, oxidized OxyR (A, lane 7).

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