Thioredoxin reductase and cytoplasmic glutathione peroxidase activity in human foetal and neonatal liver
| Autor: | Robert Hume, Michelle H. Lewin, S W Walker, Kerry Richard, A F Howie, Geoffrey J. Beckett, Fergus Nicol, John R. Arthur |
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| Rok vydání: | 2001 |
| Předmět: |
Cytoplasm
medicine.medical_specialty Thioredoxin-Disulfide Reductase Antioxidant G protein medicine.medical_treatment Thioredoxin reductase Biophysics Gestational Age Biology Biochemistry Cytosol Internal medicine medicine Humans Molecular Biology chemistry.chemical_classification Glutathione Peroxidase Cell growth Glutathione peroxidase Infant Newborn Molecular biology Oxidative Stress Endocrinology Liver chemistry Autopsy Selenoprotein Thioredoxin |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1526:237-241 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/s0304-4165(01)00133-7 |
| Popis: | Cytosolic thioredoxin reductase (TR) is an FAD-containing homodimeric selenoenzyme which, together with thioredoxin (Trx) and NADPH, forms a powerful oxidoreductase system. Cytoplasmic glutathione peroxidase (GPX-1) is a selenoprotein with antioxidant activity. The TR/Trx system has been associated with cellular processes including regulation of cell growth, and modification of activity of transcription factors. TR may also act as an antioxidant. We have measured TR activity, TR concentration, and GPX-1 activity in human hepatic cytosols from foetuses and neonates. The concentration of TR was significantly greater (P |
| Databáze: | OpenAIRE |
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