Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties
1. 1. The aim of the present work is to shed light on the way of action of hexachlorobenzene (HCB) on hepatic ferrochelatase the mitochondrial enzyme which catalyzes the last step of haem biosynthetic pathway. 2. 2. Some properties of this enzyme from normal and HCB porphyric rat liver were studied....
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v21_n2_p219_DeMolina |
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todo:paper_0020711X_v21_n2_p219_DeMolina2023-10-03T14:18:02Z Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties De Molina, M.C.R. Taira, M.C. De Viale, L.C.S.M. ferrochelatase heme hexachlorobenzene animal cell animal experiment animal model biological model enzyme assay enzyme kinetics enzyme localization female hepatic porphyria liver mitochondrion nonhuman normal value oral drug administration rat Animal Chlorobenzenes Enzyme Stability Ferrochelatase Heme Hexachlorobenzene Hydrogen-Ion Concentration Lyases Mitochondria, Liver Porphyria Rats Support, Non-U.S. Gov't 1. 1. The aim of the present work is to shed light on the way of action of hexachlorobenzene (HCB) on hepatic ferrochelatase the mitochondrial enzyme which catalyzes the last step of haem biosynthetic pathway. 2. 2. Some properties of this enzyme from normal and HCB porphyric rat liver were studied. 3. 3. The present findings indicate that HCB treatment would modify the configuration of the enzyme perhaps allowing the active center of the porphyric ferrochelatase to be more exposed. 4. 4. As a consequence it would show: (a) its higher affinity for the iron; (b) the shorter time necessary to form the intermediate enzyme-substrate, reflected both by the existence of a shorter lag and consequently a shorter pre incubation time. 5. 5. However this modification elicited by the fungicide does not alter the submitochondrial distribution of the enzyme nor the optimal conditions for its measurement. © 1989. Fil:Taira, M.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_0020711X_v21_n2_p219_DeMolina |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ferrochelatase heme hexachlorobenzene animal cell animal experiment animal model biological model enzyme assay enzyme kinetics enzyme localization female hepatic porphyria liver mitochondrion nonhuman normal value oral drug administration rat Animal Chlorobenzenes Enzyme Stability Ferrochelatase Heme Hexachlorobenzene Hydrogen-Ion Concentration Lyases Mitochondria, Liver Porphyria Rats Support, Non-U.S. Gov't |
| spellingShingle |
ferrochelatase heme hexachlorobenzene animal cell animal experiment animal model biological model enzyme assay enzyme kinetics enzyme localization female hepatic porphyria liver mitochondrion nonhuman normal value oral drug administration rat Animal Chlorobenzenes Enzyme Stability Ferrochelatase Heme Hexachlorobenzene Hydrogen-Ion Concentration Lyases Mitochondria, Liver Porphyria Rats Support, Non-U.S. Gov't De Molina, M.C.R. Taira, M.C. De Viale, L.C.S.M. Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| topic_facet |
ferrochelatase heme hexachlorobenzene animal cell animal experiment animal model biological model enzyme assay enzyme kinetics enzyme localization female hepatic porphyria liver mitochondrion nonhuman normal value oral drug administration rat Animal Chlorobenzenes Enzyme Stability Ferrochelatase Heme Hexachlorobenzene Hydrogen-Ion Concentration Lyases Mitochondria, Liver Porphyria Rats Support, Non-U.S. Gov't |
| description |
1. 1. The aim of the present work is to shed light on the way of action of hexachlorobenzene (HCB) on hepatic ferrochelatase the mitochondrial enzyme which catalyzes the last step of haem biosynthetic pathway. 2. 2. Some properties of this enzyme from normal and HCB porphyric rat liver were studied. 3. 3. The present findings indicate that HCB treatment would modify the configuration of the enzyme perhaps allowing the active center of the porphyric ferrochelatase to be more exposed. 4. 4. As a consequence it would show: (a) its higher affinity for the iron; (b) the shorter time necessary to form the intermediate enzyme-substrate, reflected both by the existence of a shorter lag and consequently a shorter pre incubation time. 5. 5. However this modification elicited by the fungicide does not alter the submitochondrial distribution of the enzyme nor the optimal conditions for its measurement. © 1989. |
| format |
JOUR |
| author |
De Molina, M.C.R. Taira, M.C. De Viale, L.C.S.M. |
| author_facet |
De Molina, M.C.R. Taira, M.C. De Viale, L.C.S.M. |
| author_sort |
De Molina, M.C.R. |
| title |
Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| title_short |
Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| title_full |
Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| title_fullStr |
Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| title_full_unstemmed |
Liver ferrochelatase from normal and hexachlorobenzene porphyric rats. Studies on their properties |
| title_sort |
liver ferrochelatase from normal and hexachlorobenzene porphyric rats. studies on their properties |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v21_n2_p219_DeMolina |
| work_keys_str_mv |
AT demolinamcr liverferrochelatasefromnormalandhexachlorobenzeneporphyricratsstudiesontheirproperties AT tairamc liverferrochelatasefromnormalandhexachlorobenzeneporphyricratsstudiesontheirproperties AT devialelcsm liverferrochelatasefromnormalandhexachlorobenzeneporphyricratsstudiesontheirproperties |
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1807322631014187008 |