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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1994
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n4_p595_deCatabbi http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n4_p595_deCatabbi |
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paper:paper_0020711X_v26_n4_p595_deCatabbi2023-06-08T14:41:14Z Studies on the active centre(s) of rat liver porphyrinogen carboxy-lyase. in vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens 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. 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n4_p595_deCatabbi 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 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. |
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 |
publishDate |
1994 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n4_p595_deCatabbi http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n4_p595_deCatabbi |
_version_ |
1768543355575205888 |