Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene

1. 1. Porphyrinogen carboxylyase from the liver of normal and hexachlorobenzene porphyric rats was subjeced to chemical modification using photo-oxidation with methylene blue, diethylpyrocarbonate, butane-2,3-dione, and phenylglyoxal. 2. 2. All of these chemicals inactivated the enzyme from both sou...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	De Catabbi, S.B., De Molina, M.D.C.R., De Viale, L.C.S.M.
Formato:	JOUR
Materias:	hexachlorobenzene uroporphyrinogen decarboxylase animal experiment animal tissue article controlled study drug toxicity enzyme active site enzyme modification liver nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Diethyl Pyrocarbonate Epoxy Compounds Female Hexachlorobenzene Histidine Hydroxylamine Hydroxylamines Liver Methylene Blue Photochemistry Porphyria Rats Rats, Inbred Strains Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogens Animalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_0020711X_v23_n7-8_p675_DeCatabbi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_0020711X_v23_n7-8_p675_DeCatabbi
record_format	dspace
spelling	todo:paper_0020711X_v23_n7-8_p675_DeCatabbi2023-10-03T14:18:06Z Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene De Catabbi, S.B. De Molina, M.D.C.R. De Viale, L.C.S.M. hexachlorobenzene uroporphyrinogen decarboxylase animal experiment animal tissue article controlled study drug toxicity enzyme active site enzyme modification liver nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Diethyl Pyrocarbonate Epoxy Compounds Female Hexachlorobenzene Histidine Hydroxylamine Hydroxylamines Liver Methylene Blue Photochemistry Porphyria Rats Rats, Inbred Strains Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogens Animalia 1. 1. Porphyrinogen carboxylyase from the liver of normal and hexachlorobenzene porphyric rats was subjeced to chemical modification using photo-oxidation with methylene blue, diethylpyrocarbonate, butane-2,3-dione, and phenylglyoxal. 2. 2. All of these chemicals inactivated the enzyme from both sources. 3. 3. Reversion of the diethylpyrocarbonate reaction with hydroxylamine as well as protection of the enzymes with uroporphyrinogen III indicated that histicline is involved at least in the first decarboxylation active site of the porphyrinogen carboxylyase, and perhaps in one or more sites where the removal of the other carboxyl groups take place. 4. 4. Arginine seems not to be at the active site of the enzyme but at its environment since two diketones alter the enzyme activity, however the substrate did not protect the enzyme from the butane-2,3-dione modification. 5. 5. Comparative studies between the enzyme from normal and porphyric animals suggest that the low enzyme activity from intoxicated animals could be due to alterations of its active centre environment produced by hexachlorobenzene treatment. This treatment seems to partially protect the active site of the porphyrinogen carboxylyase from the modification reactions. © 1991. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v23_n7-8_p675_DeCatabbi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	hexachlorobenzene uroporphyrinogen decarboxylase animal experiment animal tissue article controlled study drug toxicity enzyme active site enzyme modification liver nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Diethyl Pyrocarbonate Epoxy Compounds Female Hexachlorobenzene Histidine Hydroxylamine Hydroxylamines Liver Methylene Blue Photochemistry Porphyria Rats Rats, Inbred Strains Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogens Animalia
spellingShingle	hexachlorobenzene uroporphyrinogen decarboxylase animal experiment animal tissue article controlled study drug toxicity enzyme active site enzyme modification liver nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Diethyl Pyrocarbonate Epoxy Compounds Female Hexachlorobenzene Histidine Hydroxylamine Hydroxylamines Liver Methylene Blue Photochemistry Porphyria Rats Rats, Inbred Strains Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogens Animalia De Catabbi, S.B. De Molina, M.D.C.R. De Viale, L.C.S.M. Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
topic_facet	hexachlorobenzene uroporphyrinogen decarboxylase animal experiment animal tissue article controlled study drug toxicity enzyme active site enzyme modification liver nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Diethyl Pyrocarbonate Epoxy Compounds Female Hexachlorobenzene Histidine Hydroxylamine Hydroxylamines Liver Methylene Blue Photochemistry Porphyria Rats Rats, Inbred Strains Spectrophotometry Support, Non-U.S. Gov't Uroporphyrinogens Animalia
description	1. 1. Porphyrinogen carboxylyase from the liver of normal and hexachlorobenzene porphyric rats was subjeced to chemical modification using photo-oxidation with methylene blue, diethylpyrocarbonate, butane-2,3-dione, and phenylglyoxal. 2. 2. All of these chemicals inactivated the enzyme from both sources. 3. 3. Reversion of the diethylpyrocarbonate reaction with hydroxylamine as well as protection of the enzymes with uroporphyrinogen III indicated that histicline is involved at least in the first decarboxylation active site of the porphyrinogen carboxylyase, and perhaps in one or more sites where the removal of the other carboxyl groups take place. 4. 4. Arginine seems not to be at the active site of the enzyme but at its environment since two diketones alter the enzyme activity, however the substrate did not protect the enzyme from the butane-2,3-dione modification. 5. 5. Comparative studies between the enzyme from normal and porphyric animals suggest that the low enzyme activity from intoxicated animals could be due to alterations of its active centre environment produced by hexachlorobenzene treatment. This treatment seems to partially protect the active site of the porphyrinogen carboxylyase from the modification reactions. © 1991.
format	JOUR
author	De Catabbi, S.B. De Molina, M.D.C.R. De Viale, L.C.S.M.
author_facet	De Catabbi, S.B. De Molina, M.D.C.R. De Viale, L.C.S.M.
author_sort	De Catabbi, S.B.
title	Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
title_short	Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
title_full	Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
title_fullStr	Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
title_full_unstemmed	Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
title_sort	studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene
url	http://hdl.handle.net/20.500.12110/paper_0020711X_v23_n7-8_p675_DeCatabbi
work_keys_str_mv	AT decatabbisb studiesontheactivecentreofratliverporphyrinogencarboxylyaseinvivoeffectofhexachlorobenzene AT demolinamdcr studiesontheactivecentreofratliverporphyrinogencarboxylyaseinvivoeffectofhexachlorobenzene AT devialelcsm studiesontheactivecentreofratliverporphyrinogencarboxylyaseinvivoeffectofhexachlorobenzene
_version_	1807323636769488896

Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene

Ejemplares similares