Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase
1. 1. Uroporphyrinogen I synthetase from Rhodopseudomonas palustris has been isolated and purified. 2. 2. Assay conditions were determined. 3. 3. Sephadex G-100 column chromatography was found to increase 4-fold the degree of purification yielding a deaminase that was purified 72-fold. 4. 4. Some pr...
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| Formato: | Capítulo de libro |
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| Publicado: |
1987
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| Sumario: | 1. 1. Uroporphyrinogen I synthetase from Rhodopseudomonas palustris has been isolated and purified. 2. 2. Assay conditions were determined. 3. 3. Sephadex G-100 column chromatography was found to increase 4-fold the degree of purification yielding a deaminase that was purified 72-fold. 4. 4. Some properties of the isolated enzyme were studied. The optimal pH was about 7.6-7.8. Porphyrin formation was linear with time. The presence of several thiol reagents was found to be no essential for deaminase activity. 5. 5. Deaminase exhibited classical Michaelis-Menten kinetics Km and Vmax were estimated. 6. 6. Molecular weight determinations, by means of gel filtration on a calibrated Sephadex G-100 column, gave values of 74,000 ± 7400. © 1987. |
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| ISSN: | 03050491 |
| DOI: | 10.1016/0305-0491(87)90058-7 |