Files in this Data Supplement:

• Data Supplement - FIG. S1. Kinetics of BDCRB metabolism by hOGG1. (A) Rate of BDCRB aglycone appearance as a function of hOGG1 protein concentration following addition of 1 mM BDCRB and sampling at 20 min. (B) Time course of BDCRB aglycone appearance with 3.0 µg/mL hOGG1 protein and 1 mM BDCRB. The reaction was linear through 8 min. (C) Substrate concentration dependence to determine Km and Vmax. Rate of BDCRB aglycone formation was determined following addition of a range of substrate concentrations to 3.0 µg/mL hOGG1 protein with sampling at 8 min.
• Data Supplement - FIG. S2. Kinetics of BDCRB metabolism by mMPG. (A) Rate of BDCRB aglycone appearance as a function of mMPG protein concentration following addition of 1 mM BDCRB and sampling at 20 min. (B) Time course of BDCRB aglycone appearance with 6.0 µg/mL mMPG protein and 1 mM BDCRB. The reaction was linear through 8 min. (C) Substrate concentration dependence to determine Km and Vmax. Rate of BDCRB aglycone formation was determined following addition of a range of substrate concentrations to 6.0 µg/mL hOGG1 protein with sampling at 8 min.
• Data Supplement - FIG. S3. Dot Blot of Caco-2 cell fractions. Nuclear and supernatant fractions were blotted onto a Hybond-N+ nucleic acid transfer membrane adjacent to DNA standards ranging from 0.01 to 100 µg/mL. Following crosslinking by a Spectrolinker XL-1000, the membrane was developed with SYBR Green then visualized with UV. The results showed little DNA in the supernatant fraction, which suggested that the soluble fraction was minimally contaminated with nuclear enzymes.