Table 3.
Kinetic analyses of O-glucuronidation of 17-dihydroexemestane by human UGTs.a
| UGT | Vmax(pmol·min−1·μg−1)b | Km(μM) | Vmax/Km(nl·min−1·μg−1)b |
|---|---|---|---|
| UGT1A1 | No detectable activity | ||
| UGT1A3 | No detectable activity | ||
| UGT1A4 | 0.27 ± 0.01 | 34 ± 3.9 | 8.1 ± 0.9 |
| UGT1A5 | No detectable activity | ||
| UGT1A6 | No detectable activity | ||
| UGT1A7 | No detectable activity | ||
| UGT1A8 | 0.30 ± 0.06 | 14 ± 3.9 | 22 ± 2.1 |
| UGT1A9 | No detectable activity | ||
| UGT1A10 | 12 ± 1.8 | 124 ± 15 | 100 ± 7.9 |
| UGT2B4 | No detectable activity | ||
| UGT2B7 | No detectable activity | ||
| UGT2B10 | No detectable activity | ||
| UGT2B11 | No detectable activity | ||
| UGT2B15 | No detectable activity | ||
| UGT2B17 | 2.0 ± 0.25 | 14 ± 2.7 | 137 ± 17 |
a
All data are the mean ± standard deviation, based on three independent experiments.
b
Data are expressed per μg UGT protein, as determined by Western blot analysis.