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...
Guardado en:
Autores principales: | , |
---|---|
Publicado: |
1971
|
Materias: | |
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 |
Aporte de: |
id |
paper:paper_00052744_v227_n1_p180_Llambias |
---|---|
record_format |
dspace |
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 |
_version_ |
1768543065284280320 |