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1 M) and cytochrome P450 (SKF525A, 100 microM; ethoxyresorufin, 10 microM; metyrapone, 500 microM; pipe
2 ere compared with the commercial substrate 7-ethoxyresorufin (7-ER).
3 aiaretic acid (a lipoxygenase inhibitor) nor ethoxyresorufin (a cytochrome P450 inhibitor) altered th
4 e used to determine kcat and Km values for 7-ethoxyresorufin and phenacetin O-deethylation and the (i
5 n secretion, urea synthesis, deethylation of ethoxyresorufin (CYT P450 activity), and responsiveness
6 creening for 1A2 activity (deethylation of 7-ethoxyresorufin) identified two functional P450 hybrids
7        Reconstituted CYP1A1-Val462 catalyzed ethoxyresorufin metabolism at a slightly but significant
8 mance liquid chromatography determination of ethoxyresorufin metabolism) of cytochrome P-450 (CYP) 1A
9  environmental contaminants on cytotoxicity, ethoxyresorufin O-deethylase (EROD) activity, and mRNA e
10 453), as analyzed by both immunoblotting and ethoxyresorufin O-deethylase activity.
11 e, total CYP1A1 activity, as measured by the ethoxyresorufin O-deethylase assay, was detected in mito
12 ituted with NADPH-P450 reductase, rates of 7-ethoxyresorufin O-deethylation and phenacetin O-deethyla
13 B1 enzymatic activity was evaluated using an ethoxyresorufin O-deethylation assay in transfected HEK-
14  vitro inactivation of scup CYP1A activity 7-ethoxyresorufin O-deethylation by TCB was time dependent
15 (TK) locus, CYP1A activity was determined by ethoxyresorufin-O-deethylase (EROD) activity and qRT-PCR
16 HF-FPWs resulted in significant induction of ethoxyresorufin-O-deethylase (EROD) activity in both liv
17 romatic hydrocarbons (PAHs) for induction of ethoxyresorufin-O-deethylase (EROD) activity was assesse
18 morant hepatocytes to determine effects on 7-ethoxyresorufin-O-deethylase (EROD) activity, porphyrin
19 ryonic hepatocytes to determine effects on 7-ethoxyresorufin-O-deethylase (EROD) activity, porphyrin
20 species by determining (i) the activities of ethoxyresorufin-O-deethylase (EROD) and glutathione-S-tr
21 hpf); CYP1 activity was determined by in ovo ethoxyresorufin-o-deethylase (EROD) at 96 hpf, and cardi
22 essary for the induction of CYP1A1-dependent ethoxyresorufin-o-deethylase (EROD) enzymatic activity b
23 h several cytochrome P450 isoforms (CYPs): 7-ethoxyresorufin-O-deethylase (EROD), benzyloxy-4-[triflu
24   Moreover, corresponding enzyme activities (ethoxyresorufin-O-deethylase (EROD), CAT, SOD, and GR) w
25                              CYP1A1-mediated ethoxyresorufin-O-deethylase activity and amounts of its
26 he tested compounds induced CYP1A-associated ethoxyresorufin-O-deethylase activity in mouse embryos o
27 thyronine (T3), hepatic biotransformation (7-ethoxyresorufin-O-deethylase activity), or oxidative str
28 0 (CYP) 1A1 and 1B1 activity, as measured by ethoxyresorufin-O-deethylase activity, in cells treated
29 2 and 20 hours after shock, as determined by ethoxyresorufin-O-deethylase activity, metabolism of BaP
30 ent inhibitor of cytochrome P4501A1-mediated ethoxyresorufin-O-deethylase activity, with an IC50 of 0
31 A1 protein by Western blotting and exhibited ethoxyresorufin-O-deethylase activity; neither the CHO-n
32 xperimental results for in vitro and in vivo ethoxyresorufin-O-deethylase and vitellogenin induction
33  7-ethoxyresorufin showed a stimulation of 7-ethoxyresorufin-O-deethylation in the mixed reconstitute
34 eriments using the 1A2-preferred substrate 7-ethoxyresorufin showed a stimulation of 7-ethoxyresorufi

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