Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens

1. 1. The role of histidine on the decarboxylation of porphyrinogens of 7-, 6-, and 5-COOH III brought about by porphyrinogen carboxy-lyase (PCL) was studied. 2. 2. For this purpose hepatic PCL from normal and hexachlorobenzene (HCB) treated rats were modified with diethylpyrocarbonate. 3. 3. The re...

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Autores principales:	de Catabbi, S.C.B., de Viale, L.C.S.M.
Formato:	JOUR
Materias:	hexachlorobenzene porphyrinogen uroporphyrinogen decarboxylase animal experiment animal model article binding site carboxy terminal sequence decarboxylation drug effect enzyme active site enzyme binding enzyme modification female nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Decarboxylation Diacetyl Female Hexachlorobenzene Histidine Liver Porphyria Porphyrinogens Rats Rats, Wistar Support, Non-U.S. Gov't Animalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n4_p595_deCatabbi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_0020711X_v26_n4_p595_deCatabbi
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spelling	todo:paper_0020711X_v26_n4_p595_deCatabbi2023-10-03T14:18:08Z Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens de Catabbi, S.C.B. de Viale, L.C.S.M. hexachlorobenzene porphyrinogen uroporphyrinogen decarboxylase animal experiment animal model article binding site carboxy terminal sequence decarboxylation drug effect enzyme active site enzyme binding enzyme modification female nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Decarboxylation Diacetyl Female Hexachlorobenzene Histidine Liver Porphyria Porphyrinogens Rats Rats, Wistar Support, Non-U.S. Gov't Animalia 1. 1. The role of histidine on the decarboxylation of porphyrinogens of 7-, 6-, and 5-COOH III brought about by porphyrinogen carboxy-lyase (PCL) was studied. 2. 2. For this purpose hepatic PCL from normal and hexachlorobenzene (HCB) treated rats were modified with diethylpyrocarbonate. 3. 3. The results indicated that the enzyme from both normal and porphyric animals had histidine at the binding sites of all the porphyrinogens assayed. 4. 4. Comparative studies between the enzyme from normal and porphyric rats suggested that in vivo HCB treatment affected the active site for the decarboxylation of 7-, 6- and 5-COOH porphyrinogens III at histidine residues. 5. 5. On the other hand arginine modification by 2,3-butanedione treatment altered 5-COOH porphyrinogen III decarboxylation for both enzymes. However this amino acid was not involved at the binding site of this substrate. © 1994. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n4_p595_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 porphyrinogen uroporphyrinogen decarboxylase animal experiment animal model article binding site carboxy terminal sequence decarboxylation drug effect enzyme active site enzyme binding enzyme modification female nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Decarboxylation Diacetyl Female Hexachlorobenzene Histidine Liver Porphyria Porphyrinogens Rats Rats, Wistar Support, Non-U.S. Gov't Animalia
spellingShingle	hexachlorobenzene porphyrinogen uroporphyrinogen decarboxylase animal experiment animal model article binding site carboxy terminal sequence decarboxylation drug effect enzyme active site enzyme binding enzyme modification female nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Decarboxylation Diacetyl Female Hexachlorobenzene Histidine Liver Porphyria Porphyrinogens Rats Rats, Wistar Support, Non-U.S. Gov't Animalia de Catabbi, S.C.B. de Viale, L.C.S.M. Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
topic_facet	hexachlorobenzene porphyrinogen uroporphyrinogen decarboxylase animal experiment animal model article binding site carboxy terminal sequence decarboxylation drug effect enzyme active site enzyme binding enzyme modification female nonhuman porphyria rat Animal Arginine Binding Sites Carboxy-Lyases Decarboxylation Diacetyl Female Hexachlorobenzene Histidine Liver Porphyria Porphyrinogens Rats Rats, Wistar Support, Non-U.S. Gov't Animalia
description	1. 1. The role of histidine on the decarboxylation of porphyrinogens of 7-, 6-, and 5-COOH III brought about by porphyrinogen carboxy-lyase (PCL) was studied. 2. 2. For this purpose hepatic PCL from normal and hexachlorobenzene (HCB) treated rats were modified with diethylpyrocarbonate. 3. 3. The results indicated that the enzyme from both normal and porphyric animals had histidine at the binding sites of all the porphyrinogens assayed. 4. 4. Comparative studies between the enzyme from normal and porphyric rats suggested that in vivo HCB treatment affected the active site for the decarboxylation of 7-, 6- and 5-COOH porphyrinogens III at histidine residues. 5. 5. On the other hand arginine modification by 2,3-butanedione treatment altered 5-COOH porphyrinogen III decarboxylation for both enzymes. However this amino acid was not involved at the binding site of this substrate. © 1994.
format	JOUR
author	de Catabbi, S.C.B. de Viale, L.C.S.M.
author_facet	de Catabbi, S.C.B. de Viale, L.C.S.M.
author_sort	de Catabbi, S.C.B.
title	Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
title_short	Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
title_full	Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
title_fullStr	Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
title_full_unstemmed	Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
title_sort	studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens
url	http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n4_p595_deCatabbi
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Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens

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