| ID | 450 |
|---|---|
| Name | demethylase |
| Synonyms | DMTase; Demethylase; MBD 2; MBD2; Methyl CpG binding domain protein 2; Methyl CpG binding protein MBD2; NY CO 41; Demethylases… |
| ID | 182 |
|---|---|
| Name | endosulfan |
| CAS | 6,7,8,9,10,10-hexachloro-1,5,5a,6,9,9a-hexahydro-6,9-methano-2,4,3-benzodioxathiepin 3-oxide |
| PubMed | Abstract | RScore(About this table) |
|---|---|---|
| 2380476 | Srikanth NS, Seth PK: Alterations in xenobiotic metabolizing enzymes in brain and liver of rats coexposed to endosulfan and malathion. J Appl Toxicol. 1990 Jun;10(3):157-60. The effects of endosulfan (3 mg kg-1 body wt., i.p.) and malathion (30 mg kg-1 body wt.) and their coexposure on rat hepatic and brain xenobiotic metabolizing enzymes were investigated. Endosulfan was found to induce aminopyrine-n-demethylase (81%) and hydroxylase (59%) activities significantly in liver and to a lesser extent in brain. Malathion treatment induced malathion carboxylesterase activity in both liver (50%) and brain (22%), significantly depleted liver (35%) content with stimulation of glutathione-S-transferase (50%) and inhibited the activity of mixed-function oxidases. In the coexposed animals, malathion's inhibitory influence on mixed-function oxidases and endosulfan's inhibitory effect on malathion carboxylesterase were found to dominate, while endosulfan potentiated the activity of glutathione-S-transferase significantly in liver (69%) and brain. A similar trend of alteration in coexposed brain was found, but to a lesser extent. A significant inhibition in brain acetylcholine esterase activity (42%) in the coexposed animals suggests that endosulfan may potentiate the toxicity of malathion by interfering with and carboxylesterase routes of malathion detoxification. |
6(0,0,1,1) |