Studies on Uroporphyrinogen Biosynthesis in Pig Liver
Porphobilinogen-deaminase (PBG-D) and PBG-D-isomerase complex (PBG-D-I) from pig liver were isolated and partially purified. Uroporphyrinogen I and III formation was found to be linear with time and protein concentration. Optimal pH was about 7.4 and 7.6-7.8 for PBG-D and PBG-D-I complex, respective...
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1991
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09395075_v46_n11-12_p1101_Fumagalli http://hdl.handle.net/20.500.12110/paper_09395075_v46_n11-12_p1101_Fumagalli |
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paper:paper_09395075_v46_n11-12_p1101_Fumagalli |
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paper:paper_09395075_v46_n11-12_p1101_Fumagalli2023-06-08T15:53:26Z Studies on Uroporphyrinogen Biosynthesis in Pig Liver Association PBG-D-I Complex PBG-Deaminase Pig Liver Uroporphyrins ammonia cation multienzyme complex porphobilinogen deaminase thiol reagent uroporphyrinogen uroporphyrinogen III synthase animal article biosynthesis enzymology gel chromatography isolation and purification kinetics liver metabolism molecular weight swine Ammonia Animal Cations Chromatography, Gel Hydroxymethylbilane Synthase Kinetics Liver Molecular Weight Multienzyme Complexes Sulfhydryl Reagents Support, Non-U.S. Gov't Swine Uroporphyrinogen-III Synthase Uroporphyrinogens Porphobilinogen-deaminase (PBG-D) and PBG-D-isomerase complex (PBG-D-I) from pig liver were isolated and partially purified. Uroporphyrinogen I and III formation was found to be linear with time and protein concentration. Optimal pH was about 7.4 and 7.6-7.8 for PBG-D and PBG-D-I complex, respectively. Some properties of the isolated enzymes were studied. Molecular mass determination gave a value of 40,000 Da for PBG-D and 50,000 Da for the complex. Both enzymes exhibited classical Michaelis-Menten kinetics. Km and Vmax parameters were estimated. The effect of several divalent cations, ammonia and thiol reagents was also investigated. The differential action of some of these chemicals on PBG-D and PBG-D-I system would suggest that PBG-D and isomerase may not be only physically adjacent but actually associated. © 1991, Verlag der Zeitschrift für Naturforschung. All rights reserved. 1991 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09395075_v46_n11-12_p1101_Fumagalli http://hdl.handle.net/20.500.12110/paper_09395075_v46_n11-12_p1101_Fumagalli |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Association PBG-D-I Complex PBG-Deaminase Pig Liver Uroporphyrins ammonia cation multienzyme complex porphobilinogen deaminase thiol reagent uroporphyrinogen uroporphyrinogen III synthase animal article biosynthesis enzymology gel chromatography isolation and purification kinetics liver metabolism molecular weight swine Ammonia Animal Cations Chromatography, Gel Hydroxymethylbilane Synthase Kinetics Liver Molecular Weight Multienzyme Complexes Sulfhydryl Reagents Support, Non-U.S. Gov't Swine Uroporphyrinogen-III Synthase Uroporphyrinogens |
| spellingShingle |
Association PBG-D-I Complex PBG-Deaminase Pig Liver Uroporphyrins ammonia cation multienzyme complex porphobilinogen deaminase thiol reagent uroporphyrinogen uroporphyrinogen III synthase animal article biosynthesis enzymology gel chromatography isolation and purification kinetics liver metabolism molecular weight swine Ammonia Animal Cations Chromatography, Gel Hydroxymethylbilane Synthase Kinetics Liver Molecular Weight Multienzyme Complexes Sulfhydryl Reagents Support, Non-U.S. Gov't Swine Uroporphyrinogen-III Synthase Uroporphyrinogens Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| topic_facet |
Association PBG-D-I Complex PBG-Deaminase Pig Liver Uroporphyrins ammonia cation multienzyme complex porphobilinogen deaminase thiol reagent uroporphyrinogen uroporphyrinogen III synthase animal article biosynthesis enzymology gel chromatography isolation and purification kinetics liver metabolism molecular weight swine Ammonia Animal Cations Chromatography, Gel Hydroxymethylbilane Synthase Kinetics Liver Molecular Weight Multienzyme Complexes Sulfhydryl Reagents Support, Non-U.S. Gov't Swine Uroporphyrinogen-III Synthase Uroporphyrinogens |
| description |
Porphobilinogen-deaminase (PBG-D) and PBG-D-isomerase complex (PBG-D-I) from pig liver were isolated and partially purified. Uroporphyrinogen I and III formation was found to be linear with time and protein concentration. Optimal pH was about 7.4 and 7.6-7.8 for PBG-D and PBG-D-I complex, respectively. Some properties of the isolated enzymes were studied. Molecular mass determination gave a value of 40,000 Da for PBG-D and 50,000 Da for the complex. Both enzymes exhibited classical Michaelis-Menten kinetics. Km and Vmax parameters were estimated. The effect of several divalent cations, ammonia and thiol reagents was also investigated. The differential action of some of these chemicals on PBG-D and PBG-D-I system would suggest that PBG-D and isomerase may not be only physically adjacent but actually associated. © 1991, Verlag der Zeitschrift für Naturforschung. All rights reserved. |
| title |
Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| title_short |
Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| title_full |
Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| title_fullStr |
Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| title_full_unstemmed |
Studies on Uroporphyrinogen Biosynthesis in Pig Liver |
| title_sort |
studies on uroporphyrinogen biosynthesis in pig liver |
| publishDate |
1991 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09395075_v46_n11-12_p1101_Fumagalli http://hdl.handle.net/20.500.12110/paper_09395075_v46_n11-12_p1101_Fumagalli |
| _version_ |
1768544827516911616 |