| Name | cytochrome P450 reductase |
|---|---|
| Synonyms | CPR; CYPOR; Cytochrome P 450 reductase; Cytochrome P450 reductase; NADPH cytochrome P450 reductase; NADPH cytochrome P450 reductase; P450 (cytochrome) oxidoreductase; P450R… |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 6517596 | Fluck DS, Rappaport SM, Eastmond DA, Smith MT: Conversion of 1-naphthol to naphthoquinone metabolites by rat liver microsomes: demonstration by high-performance liquid chromatography with reductive electrochemical detection. Arch Biochem Biophys. 1984 Dec;235(2):351-8. -dependent lipid peroxidation appears to be responsible for at least part of the conversion of 1-naphthol to predominantly 1,4-naphthoquinone, and it seems likely that radical generation by -cytochrome P-450 reductase could also catalyze this conversion. 1-Naphthol therefore seems to be converted to cytotoxic naphthoquinone metabolites by mechanism (s) dependent upon the generation of free radicals in rat liver microsomes. |
81(1,1,1,1) | Details |
| 11181502 | Nelson AC, Huang W, Moody DE: Variables in human liver microsome preparation: impact on the kinetics of l-alpha-acetylmethadol (LAAM) n-demethylation and dextromethorphan O-demethylation. Drug Metab Dispos. 2001 Mar;29(3):319-25. Sedimentation plots for the marker enzymes succinate dehydrogenase, NADPH cytochrome P450 reductase (reductase), and glutathione S-transferase in the resulting premicrosomal, microsomal, and cytosolic fractions suggest that enhanced purity of microsomes can be obtained by reducing force of centrifugation, including and increasing the number of homogenization strokes. Each microsomal fraction was also assayed for protein content, cytochrome P450, cytochrome b (5) reductase, cytochrome b (5), absorbance at 420, hydroxylation, hydroxylation, dextromethorphan N- and O-demethylation, glucuronidation of morphine and 1-naphthol, and ester cleavage of p-nitrophenolacetate. |
1(0,0,0,1) | Details |
| 8442765 | Ghersi-Egea JF, Perrin R, Leininger-Muller B, Grassiot MC, Jeandel C, Floquet J, Cuny G, Siest G, Minn A: Subcellular localization of cytochrome P450, and activities of several enzymes responsible for drug metabolism in the human brain. Biochem Pharmacol. 1993 Feb 9;45(3):647-58. The other drug-metabolizing enzymes catalysing functionalization and conjugation reactions, presented the following characteristics in human brain: (i) a low activity of NADPH-cytochrome P450 reductase, which also catalyses the reduction of some xenobiotics; (ii) a high specific activity of the membrane-bound epoxide hydrolase; (iii) among the enzymes catalysing conjugation reactions, 1-naphthol-UDP-glucuronosyltransferase activity was barely or not detectable, whereas the mean glutathione-S-transferase activity was 15 times higher than the activity measured in rat brain. |
0(0,0,0,0) | Details |
| 4015675 | Doherty MA, Makowski R, Gibson GG, Cohen GM: Cytochrome P-450 dependent metabolic activation of 1-naphthol to naphthoquinones and covalent binding species. Biochem Pharmacol. 1985 Jul 1;34(13):2261-7. In the absence of and -cytochrome P-450 reductase, 1-naphthol was metabolised, in a cumene hydroperoxide- and cytochrome P-450-dependent reaction, to 1,2- and 1,4-naphthoquinone and covalently bound products. |
32(0,1,1,2) | Details |
| 2067545 | McMillan JM, Shaddock JG, Casciano DA, Arlotto MP, Leakey JE: Differential stability of drug-metabolizing enzyme activities in primary rat hepatocytes, cultured in the absence or presence of dexamethasone. Mutat Res. 1991 Jul;249(1):81-92. Cytochrome P450 and cytochrome b5 contents progressively decreased throughout the 72-h culture period to less than 25% of initial values, whereas cytochrome P450 reductase rapidly decreased by 50% during attachment, but then remained stable. Activated UDP-glucuronyltransferase activities towards 1-naphthol and declined more slowly over the 72 h than cytochrome P450 and remained at 50-60% of initial values at 72 h. |
2(0,0,0,2) | Details |
| 19023562 | Gradinaru D, Minn AL, Artur Y, Minn A, Heydel JM: Drug metabolizing enzyme expression in rat choroid plexus: effects of in vivo xenobiotics treatment. Arch Toxicol. 2009 Jun;83(6):581-6. Epub 2008 Nov 21. We present the changes in mRNA expression and enzymatic activities of UDP-glucuronosyltransferase, UGT1A6 isoform and NADPH-cytochrome P450 reductase, after in vitro treatment with xenobiotic molecules known to act in the liver as inducers or inhibitors of these drug metabolizing enzymes. Choroidal 1-naphthol glucuronidation activities were significantly induced by 3-MC and PQ administration (354 +/- 85 and 257 +/- 49 vs. 115 +/- 24 nmol/h per mg protein, in control group), whereas the other molecules were without effect. |
2(0,0,0,2) | Details |