Interaction of antimycin with cytochrome b-561. A study in secretory granules and in plasma membrane isolated from chromaffin cells of bovine adrenal medulla
| Autor: | A.N. Malviya, Dominique Aunis, A. Rendon |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Cytochrome
Biophysics Spectral shift Antimycin A Dehydrogenase Ascorbic Acid Biochemistry Structural Biology Oxidoreductase Genetics Animals Chromaffin Granules Chromaffin granule Molecular Biology Secretory granule Medulla chemistry.chemical_classification Cytochrome b561 biology Cytochrome b Cell Membrane Dithionite Cell Biology Cytochrome b Group Electron transport chain Kinetics Membrane chemistry Adrenal Medulla Spectrophotometry Chromaffin System biology.protein Cytochrome b-561 Cattle Antimycin Oxidation-Reduction Plasma membrane |
| Zdroj: | FEBS letters. 160(1-2) |
| ISSN: | 0014-5793 |
| Popis: | Cytochrome b-561 in chromaffin granules interacts with antimycin and its α-peak shifts 1 nm towards red. When chromaffin granules were treated with Triton X-100 antimycin no effect was observed. Cytochrome b-561 is located in the plasma membrane isolated from the chromaffin cells. The plasma membrane b-561 does not seem to interact with antimycin. A number of NADH or NADPH (acceptor) oxidoreductase activity has been observed in isolated plasma membrane providing clues to the origin of plasma membrane dehydrogenase. The possible role of cytochrome b561 in secretory granules other than its accredited energy conserving electron transport property is projected. |
| Databáze: | OpenAIRE |
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