Metabolism of [4-14C]oestradiol by oestrogen-induced uterine peroxidase
| Autor: | P. H. Jellinck, C. R. Lyttle |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
History
medicine.medical_specialty Hot Temperature Time Factors Gonadotropins Equine Ph optimum Endocrinology Diabetes and Metabolism Uterus Cycloheximide Education chemistry.chemical_compound Endocrinology Albumins Internal medicine medicine Animals skin and connective tissue diseases chemistry.chemical_classification Carbon Isotopes Estradiol biology Water Estrogens Hydrogen Peroxide Articles General Medicine Metabolism Hydrogen-Ion Concentration NAD Rats Computer Science Applications Subcellular distribution medicine.anatomical_structure Enzyme Peroxidases Solubility chemistry Enzyme Induction Dactinomycin NADH oxidase biology.protein Female Oxidoreductases Protein Binding Peroxidase |
| Zdroj: | Biochemical Journal. 127:481-487 |
| ISSN: | 0306-3283 |
| DOI: | 10.1042/bj1270481 |
| Popis: | 1. An enzyme that catalyses the metabolism and binding of [4-14C]oestradiol to protein and to other high-molecular-weight substances in the presence of H2O2 was shown to be absent from the uteri of immature rats and to be induced by physiological doses of oestrogen or pregnant-mare-serum gonadotrophin. 2. The pH optimum, stability to heat and other characteristics of the uterine enzyme system as well as its subcellular distribution were determined. 3. The increase in the ability of uterine preparations to convert [4-14C]oestradiol into water-soluble products as a result of oestrogen treatment was accompanied by an increase in peroxidase and NADH oxidase activities and was inhibited by actinomycin D and cycloheximide. 4. The results support the proposal that the increase in peroxidase activity after oestrogen treatment might be part of an adaptive response of the uterus permitting it to bind and inactivate oestrogens and thus limit the duration of their effect upon this target tissue. |
| Databáze: | OpenAIRE |
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