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. Author manuscript; available in PMC: 2012 Mar 15.
Published in final edited form as: Biochem Pharmacol. 2011 Jan 8;81(6):777–782. doi: 10.1016/j.bcp.2010.12.019

Table 2.

Kinetic parameters for metabolite formation from each probe substrate. Results are expressed as mean ± S.D. (n = 3-4/group)

Km (μM) Vmax (pmol/min/mg protein) CLint (ml/min/mg protein)
Ethoxyresorufin O-dealkylation (CYP1A2)
 Control 0.48 ± 0.06 53 ± 2 109 ± 13
 EB 0.45 ± 0.05 80 ± 2* 183 ± 37*
 BNF 1.35 ± 0.33* 631 ± 4** 463 ± 54**
Diclofenac 4′-hydroxylation (CYP2C6/7)
 Control 18.6 ± 5.5 432 ± 40 23.9 ± 5.2
 EB 20.0 ± 4.0 434 ± 27 24.1 ± 8.6
 PB 28.0 ± 0.6 902 ± 197* 32.3 ± 7.7*
Midazolam 1′-hydroxylation (CYP3A)
 Control 8.0 ± 6.8 178 ± 42 16.1 ± 9.2
 EB 1.7 ± 3.0 71 ± 10 7.1 ± 2.4
 DX 8.6 ± 4.3 643 ± 72** 85.2 ± 20.9*
p-Nitrophenol hydroxylation (CYP2E1)
 Control 4.8 ± 1.5 1308 ± 94 296 ± 139
 EB 7.8 ± 1.9 649 ± 38* 89 ± 24*
Bufuralol 1′-hydroxylation (CYP2D2)
 Control 5.6 ± 1.3 383 ± 30 97 ± 7
 EB 4.0 ± 0.8 962 ± 23 120 ± 16
*

p < 0.05;

**

p < 0.01 vs. control