A simple, one-step purification of cytochrome b from the bc1 complexes of bacteria
| Autor: | William E. Payne, Bernard L. Trumpower |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Oxidoreductase complex
Hemeprotein Cytochrome (Paracoccus denitrificans Rhodopseudomonas sphaeroides) Octoxynol Size-exclusion chromatography Cytochrome b Biophysics Respiratory chain Biochemistry Microbiology Polyethylene Glycols Electron Transport Complex III Structural Biology Genetics Methods Molecular Biology Integral membrane protein Triton X-114 Paracoccus denitrificans biology Bacteria Chemistry Cytochrome c Temperature Cell Biology Cytochrome b Group Combinatorial chemistry Molecular Weight Rhodopseudomonas biology.protein |
| Zdroj: | FEBS letters. 213(1) |
| ISSN: | 0014-5793 |
| Popis: | Publisher Summary This chapter describes a simple, one-step method for purification of cytochrome b from the bc 1 complexes of bacteria. Cytochrome b of the ubiquinol-cytochrome c oxidoreductase complex ( bc 1 complex) has a fundamental role in the mechanism of electron transfer through the respiratory complex. However, purification of this hydrophobic integral membrane protein is extremely difficult. The parameters that influence the efficiency of separation of bc 1 complex polypeptides in the respiratory complex are the concentration of Triton X-114 and the concentration of salt. Treatment of bacterial bc 1 complexes with Triton X-114 is an effective method for purification of cytochrome c 1 and the iron-sulfur protein. These polypeptides are present in a detergent-free aqueous phase following treatment with Triton X-114. Hence, a simple additional gel filtration step is all that should be required for efficient purification of these subunits. |
| Databáze: | OpenAIRE |
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