Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase

We characterized Uroporphyrinogen decarboxylase (UroD) (E.C. 4.1.1.37) in hepatopancreas of the crab Chasmagnathus granulatus as a first step to establish this enzyme as a possible biomarker for environmental contamination. We performed a comparative study of crab UroD with the enzyme UroD present i...

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Autores principales:	Chaufan, Rosa Gabriela, Corvi, María Martha, San Martín de Viale, Leonor Carmen, Luquet, Carlos Marcelo, Ríos de Molina, María del Carmen
Publicado:	2002
Materias:	Activation energy Crab hepatopancreas Enzymatic properties Haem Kinetic parameters Optimum pH Optimum temperature Porphyrins Rat liver Uroporphyrinogen decarboxylase 8 carboxylporphyrinogen aromatic hydrocarbon biological marker carboxyl group coproporphyrinogen oxidase liver enzyme porphyrinogen unclassified drug uroporphyrinogen decarboxylase animal experiment animal model animal tissue article chasmagnathus granulatus controlled study crab decarboxylation enzyme activity female gel chromatography hepatopancreas intoxication liver male molecular weight nonhuman pH pollutant priority journal rat temperature Animals Decapoda (Crustacea) Decarboxylation Digestive System Environmental Pollutants Hydrocarbons, Halogenated Hydrogen-Ion Concentration Kinetics Liver Porphyrinogens Rats Rats, Wistar Temperature Uroporphyrinogen Decarboxylase Chasmagnathus granulata Rattus Rattus norvegicus
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v133_n2_p251_Chaufan http://hdl.handle.net/20.500.12110/paper_10964959_v133_n2_p251_Chaufan
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_10964959_v133_n2_p251_Chaufan
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spelling	paper:paper_10964959_v133_n2_p251_Chaufan2023-06-08T16:07:03Z Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase Chaufan, Rosa Gabriela Corvi, María Martha San Martín de Viale, Leonor Carmen Luquet, Carlos Marcelo Ríos de Molina, María del Carmen Activation energy Crab hepatopancreas Enzymatic properties Haem Kinetic parameters Optimum pH Optimum temperature Porphyrins Rat liver Uroporphyrinogen decarboxylase 8 carboxylporphyrinogen aromatic hydrocarbon biological marker carboxyl group coproporphyrinogen oxidase liver enzyme porphyrinogen unclassified drug uroporphyrinogen decarboxylase animal experiment animal model animal tissue article chasmagnathus granulatus controlled study crab decarboxylation enzyme activity female gel chromatography hepatopancreas intoxication liver male molecular weight nonhuman pH pollutant priority journal rat temperature Animals Decapoda (Crustacea) Decarboxylation Digestive System Environmental Pollutants Hydrocarbons, Halogenated Hydrogen-Ion Concentration Kinetics Liver Porphyrinogens Rats Rats, Wistar Temperature Uroporphyrinogen Decarboxylase Chasmagnathus granulata Decapoda (Crustacea) Rattus Rattus norvegicus We characterized Uroporphyrinogen decarboxylase (UroD) (E.C. 4.1.1.37) in hepatopancreas of the crab Chasmagnathus granulatus as a first step to establish this enzyme as a possible biomarker for environmental contamination. We performed a comparative study of crab UroD with the enzyme UroD present in Wistar rat liver, which is known as a useful indicator of intoxication by polyhalogenated aromatic hydrocarbons (PAHs). The final products were the same in crab and rat UroD: the remaining substrate (8-carboxyl-porphyrinogen), the final product Coproporphyrinogen (4-COOH) and intermediate compounds with 7-, 6- and 5-COOH. The elimination of the second carboxyl group seems to be the rate-limiting step in this multiple decarboxylation, because large amounts of 7-COOH porphyrinogen are accumulated. The Vmax/Km ratio was 100-fold higher for rat liver UroD than for crab hepatopancreas UroD, suggesting a higher efficiency of the rat enzyme. Optimum pH for enzyme activity was 7.2 and 6.8 for crab and rat, respectively. Although both systems showed the same optimum temperature (47°C), the activation energy was clearly different, 51.5 kJ/mol for C. granulatus and 5.4 kJ/mol for Rattus norvegicus (Wistar strain). Superdex 75 gel chromatography yielded a single symmetrical peak with an apparent molecular mass of 48±3 kDa for crab hepatopancreas UroD, suggesting the existence of only one enzymatic species in C. granulatus. © 2002 Elsevier Science Inc. All rights reserved. Fil:Chaufan, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Corvi, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:San Martín de Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Luquet, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ríos de Molina, M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v133_n2_p251_Chaufan http://hdl.handle.net/20.500.12110/paper_10964959_v133_n2_p251_Chaufan
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Activation energy Crab hepatopancreas Enzymatic properties Haem Kinetic parameters Optimum pH Optimum temperature Porphyrins Rat liver Uroporphyrinogen decarboxylase 8 carboxylporphyrinogen aromatic hydrocarbon biological marker carboxyl group coproporphyrinogen oxidase liver enzyme porphyrinogen unclassified drug uroporphyrinogen decarboxylase animal experiment animal model animal tissue article chasmagnathus granulatus controlled study crab decarboxylation enzyme activity female gel chromatography hepatopancreas intoxication liver male molecular weight nonhuman pH pollutant priority journal rat temperature Animals Decapoda (Crustacea) Decarboxylation Digestive System Environmental Pollutants Hydrocarbons, Halogenated Hydrogen-Ion Concentration Kinetics Liver Porphyrinogens Rats Rats, Wistar Temperature Uroporphyrinogen Decarboxylase Chasmagnathus granulata Decapoda (Crustacea) Rattus Rattus norvegicus
spellingShingle	Activation energy Crab hepatopancreas Enzymatic properties Haem Kinetic parameters Optimum pH Optimum temperature Porphyrins Rat liver Uroporphyrinogen decarboxylase 8 carboxylporphyrinogen aromatic hydrocarbon biological marker carboxyl group coproporphyrinogen oxidase liver enzyme porphyrinogen unclassified drug uroporphyrinogen decarboxylase animal experiment animal model animal tissue article chasmagnathus granulatus controlled study crab decarboxylation enzyme activity female gel chromatography hepatopancreas intoxication liver male molecular weight nonhuman pH pollutant priority journal rat temperature Animals Decapoda (Crustacea) Decarboxylation Digestive System Environmental Pollutants Hydrocarbons, Halogenated Hydrogen-Ion Concentration Kinetics Liver Porphyrinogens Rats Rats, Wistar Temperature Uroporphyrinogen Decarboxylase Chasmagnathus granulata Decapoda (Crustacea) Rattus Rattus norvegicus Chaufan, Rosa Gabriela Corvi, María Martha San Martín de Viale, Leonor Carmen Luquet, Carlos Marcelo Ríos de Molina, María del Carmen Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
topic_facet	Activation energy Crab hepatopancreas Enzymatic properties Haem Kinetic parameters Optimum pH Optimum temperature Porphyrins Rat liver Uroporphyrinogen decarboxylase 8 carboxylporphyrinogen aromatic hydrocarbon biological marker carboxyl group coproporphyrinogen oxidase liver enzyme porphyrinogen unclassified drug uroporphyrinogen decarboxylase animal experiment animal model animal tissue article chasmagnathus granulatus controlled study crab decarboxylation enzyme activity female gel chromatography hepatopancreas intoxication liver male molecular weight nonhuman pH pollutant priority journal rat temperature Animals Decapoda (Crustacea) Decarboxylation Digestive System Environmental Pollutants Hydrocarbons, Halogenated Hydrogen-Ion Concentration Kinetics Liver Porphyrinogens Rats Rats, Wistar Temperature Uroporphyrinogen Decarboxylase Chasmagnathus granulata Decapoda (Crustacea) Rattus Rattus norvegicus
description	We characterized Uroporphyrinogen decarboxylase (UroD) (E.C. 4.1.1.37) in hepatopancreas of the crab Chasmagnathus granulatus as a first step to establish this enzyme as a possible biomarker for environmental contamination. We performed a comparative study of crab UroD with the enzyme UroD present in Wistar rat liver, which is known as a useful indicator of intoxication by polyhalogenated aromatic hydrocarbons (PAHs). The final products were the same in crab and rat UroD: the remaining substrate (8-carboxyl-porphyrinogen), the final product Coproporphyrinogen (4-COOH) and intermediate compounds with 7-, 6- and 5-COOH. The elimination of the second carboxyl group seems to be the rate-limiting step in this multiple decarboxylation, because large amounts of 7-COOH porphyrinogen are accumulated. The Vmax/Km ratio was 100-fold higher for rat liver UroD than for crab hepatopancreas UroD, suggesting a higher efficiency of the rat enzyme. Optimum pH for enzyme activity was 7.2 and 6.8 for crab and rat, respectively. Although both systems showed the same optimum temperature (47°C), the activation energy was clearly different, 51.5 kJ/mol for C. granulatus and 5.4 kJ/mol for Rattus norvegicus (Wistar strain). Superdex 75 gel chromatography yielded a single symmetrical peak with an apparent molecular mass of 48±3 kDa for crab hepatopancreas UroD, suggesting the existence of only one enzymatic species in C. granulatus. © 2002 Elsevier Science Inc. All rights reserved.
author	Chaufan, Rosa Gabriela Corvi, María Martha San Martín de Viale, Leonor Carmen Luquet, Carlos Marcelo Ríos de Molina, María del Carmen
author_facet	Chaufan, Rosa Gabriela Corvi, María Martha San Martín de Viale, Leonor Carmen Luquet, Carlos Marcelo Ríos de Molina, María del Carmen
author_sort	Chaufan, Rosa Gabriela
title	Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
title_short	Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
title_full	Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
title_fullStr	Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
title_full_unstemmed	Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
title_sort	comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase
publishDate	2002
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v133_n2_p251_Chaufan http://hdl.handle.net/20.500.12110/paper_10964959_v133_n2_p251_Chaufan
work_keys_str_mv	AT chaufanrosagabriela comparisonbetweencrabhepatopancreasandratliveruroporphyrinogendecarboxylase AT corvimariamartha comparisonbetweencrabhepatopancreasandratliveruroporphyrinogendecarboxylase AT sanmartindevialeleonorcarmen comparisonbetweencrabhepatopancreasandratliveruroporphyrinogendecarboxylase AT luquetcarlosmarcelo comparisonbetweencrabhepatopancreasandratliveruroporphyrinogendecarboxylase AT riosdemolinamariadelcarmen comparisonbetweencrabhepatopancreasandratliveruroporphyrinogendecarboxylase
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Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase

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