Publication: Cytochrome P450s
| dc.contributor.author | Amnuay Thithapandha | en_US |
| dc.contributor.author | อำนวย ฐิตาพันธ์ | en_US |
| dc.contributor.other | Mahidol University. Faculty of Medicine Ramathibodi Hospital. Office of Academic Affairs | en_US |
| dc.date.accessioned | 2022-10-11T06:10:25Z | |
| dc.date.available | 2022-10-11T06:10:25Z | |
| dc.date.created | 2022-10-11 | |
| dc.date.issued | 2009 | |
| dc.description.abstract | Cytochrome P450s or CYPs are heme proteins found in several organs but in high amount in both mammalian and human livers. The heme iron binds oxygen in the CYP active site, where oxidation of xenobiotics and endogenous compounds occurs. Electrons are supplied by the enzyme NADPH-cyto- chrome P450 oxidoreductase and its cofactor, NADPH. Metabolism of a substrate by a CYP consumes one molecule of O2 and produces on oxidized substrate and a molecule of water (Fig. 1). Depending on the nature of the substrate, the reaction for some CYPs is partially “uncoupled,” consuming more Oz than substrate metabolized and producing “activated oxygen” or O2 which is usually converted to water by the enzyme superoxide dismutase (SOD). | en_US |
| dc.identifier.citation | Ramathibodi Medical Journal. Vol. 32, No. 2 (Apr-Jun 2009), 101-104 | |
| dc.identifier.issn | 0125-3611 (Print) | |
| dc.identifier.issn | 2651-0561 (Online) | |
| dc.identifier.uri | https://repository.li.mahidol.ac.th/handle/123456789/79892 | |
| dc.language.iso | eng | en_US |
| dc.rights.holder | Office of Academic Affairs Faculty of Medicine Ramathibodi Hospital Mahidol University | en_US |
| dc.subject | Cytochrome | en_US |
| dc.title | Cytochrome P450s | en_US |
| dc.type | Article | en_US |
| dspace.entity.type | Publication | |
| mods.location.url | https://he02.tci-thaijo.org/index.php/ramajournal/article/view/175339/125405 |