. 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)

	K_m (μM)	V_max (pmol/min/mg protein)	CL_int (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