|Title||[Molecular organization of the reductase complex in adrenal cortex mitochondria. Study using bifunctional reagents].|
|Publication Type||Journal Article|
|Year of Publication||1986|
|Authors||Usanov, SA, Turko, IV, Chashchin, VL, Akhrem, AA|
|Date Published||1986 Feb|
|Keywords||Adrenal Cortex, Adrenodoxin, Animals, Binding Sites, Cattle, Chromatography, Gel, Cross-Linking Reagents, Cytochrome P-450 Enzyme System, Electron Transport, Electrophoresis, Polyacrylamide Gel, Ferredoxin-NADP Reductase, Mitochondria, NADH, NADPH Oxidoreductases, NADP|
The water-soluble carbodiimide, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, homobifunctional reagent 3,3'-dithiobis (succinimidyl propionate), and heterobifunctional reagent N-succinimidyl 3-(2-pyridyldithio) propionate have been used to cross-link adrenodoxin reductase and adrenodoxin, components of steroidogenic electron transfer system. Though maximal yield of the cross-linked complex was achieved with the water-soluble carbodiimide, this complex was inactive in the electron transfer from NADPH to cytochrome P-450. The functionally active complex was formed with N-succinimidyl 3-(2-pyridyldithio) propionate. The complex was purified to the apparent homogeneity and shown to be able to mediate the electron transfer. The data obtained indicate existence of different binding sites on adrenodoxin responsible for the adrenodoxin reductase and cytochrome P-450scc binding and do not contradict to the model of the steroidogenic electron transfer in an organized complex.
|Alternate Journal||Bioorg. Khim.|