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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| Formato: | Artículo publishedVersion |
| Lenguaje: | Inglés |
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1971
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias |
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paperaa:paper_00052744_v227_n1_p180_Llambias2023-06-12T16:41:14Z Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components BBA - Enzymology 1971;227(1):180-191 Llambías, E.B.C. Del C. Batlle, A.M. 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 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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) |
| language |
Inglés |
| orig_language_str_mv |
eng |
| 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, E.B.C. Del C. Batlle, A.M. 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. |
| format |
Artículo Artículo publishedVersion |
| author |
Llambías, E.B.C. Del C. Batlle, A.M. |
| author_facet |
Llambías, E.B.C. Del C. Batlle, A.M. |
| author_sort |
Llambías, E.B.C. |
| 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 |
http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias |
| work_keys_str_mv |
AT llambiasebc porphyrinbiosynthesisviiiavianerythrocyteporphobilinogendeaminaseuroporphyrinogeniiicosynthetaseitspurificationpropertiesandtheseparationofitscomponents AT delcbatlleam porphyrinbiosynthesisviiiavianerythrocyteporphobilinogendeaminaseuroporphyrinogeniiicosynthetaseitspurificationpropertiesandtheseparationofitscomponents |
| _version_ |
1769810207682068480 |