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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Autores principales: Sancovich, H.A., Ferramola, A.M., Del Batlle, C.A.M.
Formato: JOUR
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: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 todo:paper_NIS18664_v26_n5_p379_Sancovich
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spelling todo:paper_NIS18664_v26_n5_p379_Sancovich2023-10-03T16:46:10Z Studies on cow liver porphobilinogen deaminase Sancovich, H.A. Ferramola, A.M. Del Batlle, C.A.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
Sancovich, H.A.
Ferramola, A.M.
Del Batlle, C.A.M.
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.
format JOUR
author Sancovich, H.A.
Ferramola, A.M.
Del Batlle, C.A.M.
author_facet Sancovich, H.A.
Ferramola, A.M.
Del Batlle, C.A.M.
author_sort Sancovich, H.A.
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
url http://hdl.handle.net/20.500.12110/paper_NIS18664_v26_n5_p379_Sancovich
work_keys_str_mv AT sancovichha studiesoncowliverporphobilinogendeaminase
AT ferramolaam studiesoncowliverporphobilinogendeaminase
AT delbatllecam studiesoncowliverporphobilinogendeaminase
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