Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components

1. 1. A method for the isolation and purification of porphobilinogenase, porphobilinogen deaminase and uroporphyrinogen isomerase from avian erythrocytes is described. 2. 2. Some properties of the isolated enzymes were studied. The optimal pH for porphobilinogenase and deaminase was 7.4. Purified po...

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Autores principales: Llambías, Elena Blanca Cecilia, Batlle, Alcira María del Carmen
Publicado: 1971
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p180_Llambias
http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias
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spelling paper:paper_00052744_v227_n1_p180_Llambias2023-06-08T14:29:54Z Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components Llambías, Elena Blanca Cecilia Batlle, Alcira María del Carmen 4 chloromercuribenzoic acid adenine nucleotide adenosine triphosphate ammonia ammonium derivative Carboxy Lyases carboxylyase cysteine dicarboxylic acid animal article chicken dialysis ion exchange chromatography isolation and purification metabolism Adenine Nucleotides Adenosine Triphosphate Ammonia Ammonium Compounds Animal Carboxy-Lyases Chickens Chloromercuribenzoates Chromatography, DEAE-Cellulose Cysteine Dialysis Dicarboxylic Acids 1. 1. A method for the isolation and purification of porphobilinogenase, porphobilinogen deaminase and uroporphyrinogen isomerase from avian erythrocytes is described. 2. 2. Some properties of the isolated enzymes were studied. The optimal pH for porphobilinogenase and deaminase was 7.4. Purified porphobilinogenase was resolved into three bands on starch gel electrophoresis. The molecular weight of the purified enzymes was determined by gel filtration. The presence of porphobilinogen or NH4 + at certain concentrations afforded protection against heat inactivation of isomerase, the heat labile enzyme. Initial porphyrin formation by porphobilinogenase was linear with time. 3. 3. The action of various compounds added to the system was studied. Thiol reagents inhibited both porphobilinogenase and deaminase, indicating the presence of thiol groups essential for activity. NH4 +, hydroxylamine, adenine, ADP, ATP, some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited deaminase. © 1971. Fil:Llambías, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1971 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p180_Llambias http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 4 chloromercuribenzoic acid
adenine nucleotide
adenosine triphosphate
ammonia
ammonium derivative
Carboxy Lyases
carboxylyase
cysteine
dicarboxylic acid
animal
article
chicken
dialysis
ion exchange chromatography
isolation and purification
metabolism
Adenine Nucleotides
Adenosine Triphosphate
Ammonia
Ammonium Compounds
Animal
Carboxy-Lyases
Chickens
Chloromercuribenzoates
Chromatography, DEAE-Cellulose
Cysteine
Dialysis
Dicarboxylic Acids
spellingShingle 4 chloromercuribenzoic acid
adenine nucleotide
adenosine triphosphate
ammonia
ammonium derivative
Carboxy Lyases
carboxylyase
cysteine
dicarboxylic acid
animal
article
chicken
dialysis
ion exchange chromatography
isolation and purification
metabolism
Adenine Nucleotides
Adenosine Triphosphate
Ammonia
Ammonium Compounds
Animal
Carboxy-Lyases
Chickens
Chloromercuribenzoates
Chromatography, DEAE-Cellulose
Cysteine
Dialysis
Dicarboxylic Acids
Llambías, Elena Blanca Cecilia
Batlle, Alcira María del Carmen
Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
topic_facet 4 chloromercuribenzoic acid
adenine nucleotide
adenosine triphosphate
ammonia
ammonium derivative
Carboxy Lyases
carboxylyase
cysteine
dicarboxylic acid
animal
article
chicken
dialysis
ion exchange chromatography
isolation and purification
metabolism
Adenine Nucleotides
Adenosine Triphosphate
Ammonia
Ammonium Compounds
Animal
Carboxy-Lyases
Chickens
Chloromercuribenzoates
Chromatography, DEAE-Cellulose
Cysteine
Dialysis
Dicarboxylic Acids
description 1. 1. A method for the isolation and purification of porphobilinogenase, porphobilinogen deaminase and uroporphyrinogen isomerase from avian erythrocytes is described. 2. 2. Some properties of the isolated enzymes were studied. The optimal pH for porphobilinogenase and deaminase was 7.4. Purified porphobilinogenase was resolved into three bands on starch gel electrophoresis. The molecular weight of the purified enzymes was determined by gel filtration. The presence of porphobilinogen or NH4 + at certain concentrations afforded protection against heat inactivation of isomerase, the heat labile enzyme. Initial porphyrin formation by porphobilinogenase was linear with time. 3. 3. The action of various compounds added to the system was studied. Thiol reagents inhibited both porphobilinogenase and deaminase, indicating the presence of thiol groups essential for activity. NH4 +, hydroxylamine, adenine, ADP, ATP, some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited deaminase. © 1971.
author Llambías, Elena Blanca Cecilia
Batlle, Alcira María del Carmen
author_facet Llambías, Elena Blanca Cecilia
Batlle, Alcira María del Carmen
author_sort Llambías, Elena Blanca Cecilia
title Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title_short Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title_full Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title_fullStr Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title_full_unstemmed Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title_sort porphyrin biosynthesis. viii. avian erythrocyte porphobilinogen deaminase-uroporphyrinogen iii cosynthetase, its purification, properties and the separation of its components
publishDate 1971
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p180_Llambias
http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias
work_keys_str_mv AT llambiaselenablancacecilia porphyrinbiosynthesisviiiavianerythrocyteporphobilinogendeaminaseuroporphyrinogeniiicosynthetaseitspurificationpropertiesandtheseparationofitscomponents
AT batllealciramariadelcarmen porphyrinbiosynthesisviiiavianerythrocyteporphobilinogendeaminaseuroporphyrinogeniiicosynthetaseitspurificationpropertiesandtheseparationofitscomponents
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