| Name | cytochrome P450 (protein family or complex) |
|---|---|
| Synonyms | cytochrome P450; cytochrome P 450; CYP450; CYP 450 |
| Name | mercuric chloride |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2059905 | Belanger PM, St-Hilaire S: The characteristics of the microsomal hydroxylation of . Can J Physiol Pharmacol. 1991 Mar;69(3):400-5. alpha-naphthoflavone, phenelzine, mercuric chloride, and significantly inhibited the reaction indicating the involvement of the cytochrome P-450 monooxygenase. |
83(1,1,1,3) | Details |
| 2319474 | Roy D, Snodgrass WR: Covalent binding of phenytoin to protein and modulation of phenytoin metabolism by thiols in A/J mouse liver microsomes. J Pharmacol Exp Ther. 1990 Mar;252(3):895-900. Covalent binding was inhibited by inhibitors of cytochrome P-450. Low molecular weight thiols (GSH, and a thiol generator (methylthiazolidine carboxylate), and thiol modifying agents (N-ethylmaleimide, mercuric chloride and diamide) significantly inhibited covalent binding. |
2(0,0,0,2) | Details |
| 1489528 | Yang M, Luo Y, Liu Y: Potential use of luminol-dependent chemiluminescence for estimation of free radicals produced in hepatic microsomes and reconstituted cytochrome P-450 systems. Biomed Environ Sci. 1992 Dec;5(4):336-48. A concentration of 24 mumol.L-1 cadmium and 2.5 mumol.L-1 mercuric chloride also inhibited the signal significantly as compared with the control. |
2(0,0,0,2) | Details |
| 11240397 | Kaliman PA, Nikitchenko IV, Sokol OA, Strel'chenko EV: Regulation of heme oxygenase activity in rat liver during oxidative stress induced by and mercury Biochemistry. 2001 Jan;66(1):77-82. Activities of heme oxygenase and tryptophan-2,3-dioxygenase and cytochrome P450 content in liver as well as absorption of the Soret band and optical density at 280 nm in serum were determined 2 and 24 h after administration of HgCl (2) and CoCl (2) and after co-administration of the metal salts with |
2(0,0,0,2) | Details |
| 11240372 | Jiang H, Ichikawa M, Furukawa A, Tomita S, Ohnishi T, Ichikawa Y: The optical interconversion of the P-450 and P-420 forms of neuronal synthase: effects of mercury and urea. Int J Biochem Cell Biol. 2001 Feb;33(2):155-62. These results suggested that nNOS was more stable as to exposure to mercury or urea in comparison to microsomal cytochrome P-450, which may be due to the different heme environment and protein structure. |
1(0,0,0,1) | Details |