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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todo:paper_03050491_v87_n3_p601_Kotler2023-10-03T15:21:20Z Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase Kotler, M.L. Fumagalli, S.A. Juknat, A.A. del C. Batlle, A.M. 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. Fil:Kotler, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Fumagalli, S.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Juknat, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03050491_v87_n3_p601_Kotler |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| description |
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. |
| format |
JOUR |
| author |
Kotler, M.L. Fumagalli, S.A. Juknat, A.A. del C. Batlle, A.M. |
| spellingShingle |
Kotler, M.L. Fumagalli, S.A. Juknat, A.A. del C. Batlle, A.M. Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| author_facet |
Kotler, M.L. Fumagalli, S.A. Juknat, A.A. del C. Batlle, A.M. |
| author_sort |
Kotler, M.L. |
| title |
Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| title_short |
Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| title_full |
Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| title_fullStr |
Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| title_full_unstemmed |
Porphyrin biosynthesis in Rhodopseudomonas palustris-VIII. Purification and properties of deaminase |
| title_sort |
porphyrin biosynthesis in rhodopseudomonas palustris-viii. purification and properties of deaminase |
| url |
http://hdl.handle.net/20.500.12110/paper_03050491_v87_n3_p601_Kotler |
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