Separation of enzymically active bovine cytochrome c oxidase monomers and dimers by high performance liquid chromatography
| Autor: | K. M. C. Sinjorgo, B.F. Van Gelder, Theodorus B. M. Hakvoort, Anton O. Muijsers |
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| Přispěvatelé: | Other departments |
| Rok vydání: | 1985 |
| Předmět: |
Stereochemistry
Macromolecular Substances Ionic bonding Cytochrome c Group Biochemistry Inorganic Chemistry Electron Transport Complex IV chemistry.chemical_compound Cytochrome c oxidase Organic chemistry Animals Chromatography High Pressure Liquid Oxidase test biology Cytochrome c peroxidase Cytochrome c Myocardium Osmolar Concentration Kinetics Monomer chemistry Covalent bond Ionic strength Spectrophotometry biology.protein Cattle |
| Zdroj: | Journal of inorganic biochemistry, 23(3-4), 381-388. Elsevier Inc. |
| ISSN: | 0162-0134 |
| Popis: | The aggregation state of two types of bovine heart cytochrome c oxidase preparations in the presence of laurylmaltoside was investigated by high performance liquid chromatography in two buffers of ionic strengths of 388 mM and 45 mM, respectively. At high ionic strength, it was found that the Fowler cytochrome c oxidase preparation was monomeric (Mr = 2 X 10(5)), while monomers and dimers (2 X aa3, Mr = 4 X 10(5)) could be isolated from the Yonetani preparation. Under these conditions there was no rapid equilibrium between the two forms. Covalent cytochrome c oxidase-cytochrome c complexes were largely dimeric, and addition of ascorbate and cytochrome c to the oxidase also promoted dimerization. At low ionic strength (I = 45 mM) in the presence of laurylmaltoside the oxidase and the covalent complex with cytochrome c were largely monomeric. In the steady-state oxidation of ferrous horse heart cytochrome c, the monomeric enzyme displayed biphasic kinetics at I = 45 mM. This suggests that the presence of high- and low-affinity reactions is an intrinsic property of the cytochrome c oxidase monomer. |
| Databáze: | OpenAIRE |
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