Porphobilinogenase from Rhodopseudomonas palustris
1. 1. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the am...
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todo:paper_03050491_v92_n2_p291_Juknat2023-10-03T15:21:21Z Porphobilinogenase from Rhodopseudomonas palustris Juknat, A.A. Kotler, M.L. Koopmann, G.E. Batlle, A.M.d.C. ammonia lyase Ammonia Lyases porphobilinogenase article enzymology gel chromatography isolation and purification kinetics metabolism molecular weight pH Rhodopseudomonas Ammonia-Lyases Chromatography, Gel Hydrogen-Ion Concentration Kinetics Molecular Weight Rhodopseudomonas Support, Non-U.S. Gov't 1. 1. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the amount of PBG consumed. 3. 3. Cyclotetramerization rate and distribution of reaction products were not affected either by the presence or absence of oxygen. 4. 4. Two PBGase active species of mol. wt 115,000 and 50,000 were found, by means of gel filtration through a calibrated Sephadex G-100 column. 5. 5. Kinetic data show the existence of positive cooperative effects for porphyrin formation, while a hyperbolic behaviour for PBG consumption was observed. © 1989. Fil:Juknat, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kotler, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.d.C. 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_v92_n2_p291_Juknat |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ammonia lyase Ammonia Lyases porphobilinogenase article enzymology gel chromatography isolation and purification kinetics metabolism molecular weight pH Rhodopseudomonas Ammonia-Lyases Chromatography, Gel Hydrogen-Ion Concentration Kinetics Molecular Weight Rhodopseudomonas Support, Non-U.S. Gov't |
| spellingShingle |
ammonia lyase Ammonia Lyases porphobilinogenase article enzymology gel chromatography isolation and purification kinetics metabolism molecular weight pH Rhodopseudomonas Ammonia-Lyases Chromatography, Gel Hydrogen-Ion Concentration Kinetics Molecular Weight Rhodopseudomonas Support, Non-U.S. Gov't Juknat, A.A. Kotler, M.L. Koopmann, G.E. Batlle, A.M.d.C. Porphobilinogenase from Rhodopseudomonas palustris |
| topic_facet |
ammonia lyase Ammonia Lyases porphobilinogenase article enzymology gel chromatography isolation and purification kinetics metabolism molecular weight pH Rhodopseudomonas Ammonia-Lyases Chromatography, Gel Hydrogen-Ion Concentration Kinetics Molecular Weight Rhodopseudomonas Support, Non-U.S. Gov't |
| description |
1. 1. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the amount of PBG consumed. 3. 3. Cyclotetramerization rate and distribution of reaction products were not affected either by the presence or absence of oxygen. 4. 4. Two PBGase active species of mol. wt 115,000 and 50,000 were found, by means of gel filtration through a calibrated Sephadex G-100 column. 5. 5. Kinetic data show the existence of positive cooperative effects for porphyrin formation, while a hyperbolic behaviour for PBG consumption was observed. © 1989. |
| format |
JOUR |
| author |
Juknat, A.A. Kotler, M.L. Koopmann, G.E. Batlle, A.M.d.C. |
| author_facet |
Juknat, A.A. Kotler, M.L. Koopmann, G.E. Batlle, A.M.d.C. |
| author_sort |
Juknat, A.A. |
| title |
Porphobilinogenase from Rhodopseudomonas palustris |
| title_short |
Porphobilinogenase from Rhodopseudomonas palustris |
| title_full |
Porphobilinogenase from Rhodopseudomonas palustris |
| title_fullStr |
Porphobilinogenase from Rhodopseudomonas palustris |
| title_full_unstemmed |
Porphobilinogenase from Rhodopseudomonas palustris |
| title_sort |
porphobilinogenase from rhodopseudomonas palustris |
| url |
http://hdl.handle.net/20.500.12110/paper_03050491_v92_n2_p291_Juknat |
| work_keys_str_mv |
AT juknataa porphobilinogenasefromrhodopseudomonaspalustris AT kotlerml porphobilinogenasefromrhodopseudomonaspalustris AT koopmannge porphobilinogenasefromrhodopseudomonaspalustris AT batlleamdc porphobilinogenasefromrhodopseudomonaspalustris |
| _version_ |
1807318396708061184 |