EC Number   |
|---|
    1.3.5.1 | - |
| 1.3.5.1 | a purification procedure is established to enrich the protein 24fold via a combination of anion exchange and gel filtration chromatography with a yield of 36% of the initial activity in the periplasm extract |
| 1.3.5.1 | and reconstitution into proteoliposomes |
| 1.3.5.1 | by selective resolution of complex II with chaotropic salts |
| 1.3.5.1 | comparison of methods |
| 1.3.5.1 | enzyme from membranes of strain 3G18, expressed from low copy plasmid |
| 1.3.5.1 | from complex II, i.e. EC 1.3.5.1 |
| 1.3.5.1 | from EC 1.3.5.1 |
| 1.3.5.1 | isolation from the soluble cytochrome b-c1 complex of the mitochondrial protein, which converts soluble succinate dehydrogenase into succinate-ubiquinone oxidoreductase using two different methods, method 1: treatment with Triton X-100 in the presence of urea, column chromatography on calcium phosphate and ammonium sulfate fractionation, method 2: ammonium acetate fractionation in the presence of deoxycholate, ammonium sulfate fractionation in the presence of urea, and differential centrifugation |
| 1.3.5.1 | native enzyme by ammonium sulfate fractionation and gel filtration followed by anion exchange chromatography |
