Thyroxine deiodination associated with NADPH-dependent lipid peroxidation in a submicrosomal system
| Autor: | Kunihiko Suwa, Minoru Nakano |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
medicine.medical_specialty
Lipoproteins Size-exclusion chromatography Reductase General Biochemistry Genetics and Molecular Biology Lipid peroxidation chemistry.chemical_compound Internal medicine medicine Animals NADPH-Ferrihemoprotein Reductase Chromatography Malondialdehyde Rats Thyroxine Endocrinology chemistry Biochemistry Sephadex Microsome Chromatography Gel Microsomes Liver Ferric Trypsin Digestion Peptides NADP medicine.drug Iodine |
| Zdroj: | Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.). 150(2) |
| ISSN: | 0037-9727 |
| Popis: | A lipoprotein present in trypsin-treated microsomes can be oxidized with formation of malondialdehyde in a system which contains NADPH, ferric ion-ADP complex, NADPH-cytochrome c reductase and a factor. This factor, a mixture of peptides, can be isolated from hepatic microsomes by trypsin digestion and successive gel filtration through Sephadex G-100 and G-25 columns. Lipid peroxidation in this system catalyzes the deiodination of thyroxine, as does NADPH-dependent lipid peroxidation in fresh hepatic microsomes. Thyroxine inhibits lipid peroxidation as it is deiodinated in this system. |
| Databáze: | OpenAIRE |
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