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...

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Publicado: 1991
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rat
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v23_n7-8_p675_DeCatabbi
http://hdl.handle.net/20.500.12110/paper_0020711X_v23_n7-8_p675_DeCatabbi
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spelling paper:paper_0020711X_v23_n7-8_p675_DeCatabbi2025-07-30T17:23:39Z Studies on the active centre of rat liver porphyrinogen carboxylyase in vivo effect of hexachlorobenzene 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. 1991 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v23_n7-8_p675_DeCatabbi 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
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.
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
publishDate 1991
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v23_n7-8_p675_DeCatabbi
http://hdl.handle.net/20.500.12110/paper_0020711X_v23_n7-8_p675_DeCatabbi
_version_ 1840323193301106688