Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100
| Autor: | Volker Thiele, Udo Schwuléra, Hans‐Werner Müller, Klaus Dose, Erwin Schneider, Klaus Rittinghaus |
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| Rok vydání: | 1979 |
| Předmět: |
Macromolecular Substances
Size-exclusion chromatography Rhodospirillum rubrum Biochemistry Polyethylene Glycols Substrate Specificity Divalent chemistry.chemical_compound Moiety Amino Acids Sodium dodecyl sulfate Adenosine Triphosphatases chemistry.chemical_classification Chromatography Molecular mass biology Chemistry Isoelectric focusing Bacterial Chromatophores biology.organism_classification Molecular Weight Kinetics Oxidative Phosphorylation Coupling Factors Triton X-100 Oligomycins |
| Zdroj: | European Journal of Biochemistry. 97:511-517 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1979.tb13139.x |
| Popis: | 1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5. The amino acid composition of the F0F1 complex is compared with the data obtained for the F1 moiety of the enzyme. 6. Quantitative data on the sensitivity to N,N'-dicyclohexyl-carbodiimide as well as kinetic parameters, regarding substrate specificity and dependence of ATPase activity on divalent cations, are reported. |
| Databáze: | OpenAIRE |
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