Identification of thiol:protein disulfide oxidoreductase activity in cultured human fibroblasts: Dependence of enzyme activity on growth conditions
| Autor: | Patrick P. Chang, Jack E. Dixon, John E. Morin, Joel Moss |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Immunoprecipitation
Biophysics Protein-disulfide reductase (glutathione) Biochemistry Protein disulfide oxidoreductase activity Oxidoreductase medicine Humans Insulin Fibroblast Molecular Biology Cells Cultured Skin chemistry.chemical_classification biology Chemistry Membrane Proteins Protein Disulfide Reductase (Glutathione) Cell Biology Fibroblasts Molecular biology Enzyme assay Culture Media Chemically defined medium Blood medicine.anatomical_structure biology.protein Thiol Oxidoreductases |
| Zdroj: | Biochemical and Biophysical Research Communications. 111:872-877 |
| ISSN: | 0006-291X |
| Popis: | Thiol:protein disulfide oxidoreductase activity was assayed in extracts of cultured normal human skin fibroblasts. Enzyme activity in confluent fibroblasts was dependent on growth conditions. In serum-deprived fibroblasts grown in minimal medium enzyme activity was approximately 40% of that observed in fibroblasts maintained in medium supplemented with 10% fetal calf serum. In fibroblasts cultured in medium supplemented only with insulin, activity was 35% greater than that in fibroblasts cultured in unsupplemented defined medium. Antibodies raised against purified bovine liver thiol:protein disulfide oxidoreductase immunoprecipitated all of the activity present in fibroblast extracts. The thiol:protein disulfide oxidoreductase from human fibroblasts thus appears to share antigenic determinants with the bovine liver enzyme. The human fibroblast may serve as an in vitro model to study the regulation of the oxidoreductase. |
| Databáze: | OpenAIRE |
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