Studies on cow liver porphobilinogen deaminase

Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single band on starch and polyacrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B10-Gel P-100 gave valu...

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Publicado:	1976
Materias:	porphobilinogen deaminase animal experiment cattle in vitro study liver Ammonia-Lyases Animal Cations, Divalent Cattle Chelating Agents Electrophoresis, Polyacrylamide Gel Electrophoresis, Starch Gel Female Heat Hydroxymethylbilane Synthase Liver Molecular Weight Sulfhydryl Reagents
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich http://hdl.handle.net/20.500.12110/paper_NIS18664_v26_n5_p379_Sancovich
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_NIS18664_v26_n5_p379_Sancovich
record_format	dspace
spelling	paper:paper_NIS18664_v26_n5_p379_Sancovich2023-06-08T16:39:51Z Studies on cow liver porphobilinogen deaminase porphobilinogen deaminase animal experiment cattle in vitro study liver Ammonia-Lyases Animal Cations, Divalent Cattle Chelating Agents Electrophoresis, Polyacrylamide Gel Electrophoresis, Starch Gel Female Heat Hydroxymethylbilane Synthase Liver Molecular Weight Sulfhydryl Reagents Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single band on starch and polyacrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B10-Gel P-100 gave values of 40,000 ± 4,000. Data obtained suggest that cow liver deaminase exists as a single polypeptide chain. Heating partially purified preparations of deaminase resulted in an enhancement of activity. Added cosynthetase to these fractions increased the percentage of uroporphyrinogen III formed but also diminished total uroporphyrinogens synthesis. The action of several compounds added to the system was studied. Thiol reagents and divalent metals as Hg2+, Pb2+, Cd2+ inhibited deaminase, indicating the presence of thiol groups essential for activity, probably involved in the cyclization step. Certain concentrations of sodium, potassium and magnesium salts enhanced activity. Several chelators tested were without effect on the deaminase. Some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited the enzyme. 1976 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich http://hdl.handle.net/20.500.12110/paper_NIS18664_v26_n5_p379_Sancovich
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	porphobilinogen deaminase animal experiment cattle in vitro study liver Ammonia-Lyases Animal Cations, Divalent Cattle Chelating Agents Electrophoresis, Polyacrylamide Gel Electrophoresis, Starch Gel Female Heat Hydroxymethylbilane Synthase Liver Molecular Weight Sulfhydryl Reagents
spellingShingle	porphobilinogen deaminase animal experiment cattle in vitro study liver Ammonia-Lyases Animal Cations, Divalent Cattle Chelating Agents Electrophoresis, Polyacrylamide Gel Electrophoresis, Starch Gel Female Heat Hydroxymethylbilane Synthase Liver Molecular Weight Sulfhydryl Reagents Studies on cow liver porphobilinogen deaminase
topic_facet	porphobilinogen deaminase animal experiment cattle in vitro study liver Ammonia-Lyases Animal Cations, Divalent Cattle Chelating Agents Electrophoresis, Polyacrylamide Gel Electrophoresis, Starch Gel Female Heat Hydroxymethylbilane Synthase Liver Molecular Weight Sulfhydryl Reagents
description	Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single band on starch and polyacrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B10-Gel P-100 gave values of 40,000 ± 4,000. Data obtained suggest that cow liver deaminase exists as a single polypeptide chain. Heating partially purified preparations of deaminase resulted in an enhancement of activity. Added cosynthetase to these fractions increased the percentage of uroporphyrinogen III formed but also diminished total uroporphyrinogens synthesis. The action of several compounds added to the system was studied. Thiol reagents and divalent metals as Hg2+, Pb2+, Cd2+ inhibited deaminase, indicating the presence of thiol groups essential for activity, probably involved in the cyclization step. Certain concentrations of sodium, potassium and magnesium salts enhanced activity. Several chelators tested were without effect on the deaminase. Some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited the enzyme.
title	Studies on cow liver porphobilinogen deaminase
title_short	Studies on cow liver porphobilinogen deaminase
title_full	Studies on cow liver porphobilinogen deaminase
title_fullStr	Studies on cow liver porphobilinogen deaminase
title_full_unstemmed	Studies on cow liver porphobilinogen deaminase
title_sort	studies on cow liver porphobilinogen deaminase
publishDate	1976
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich http://hdl.handle.net/20.500.12110/paper_NIS18664_v26_n5_p379_Sancovich
_version_	1769175828573192192

Studies on cow liver porphobilinogen deaminase

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