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

Autores
Llambías, E.B.C.; Del C. Batlle, A.M.
Año de publicación
1971
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fuente
BBA - Enzymology 1971;227(1):180-191
Materia
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
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00052744_v227_n1_p180_Llambias
Acceder
id BDUBAFCEN_b1342d67ad0d6dd0fe7920f535e30361
oai_identifier_str paperaa:paper_00052744_v227_n1_p180_Llambias
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its componentsLlambías, E.B.C.Del C. Batlle, A.M.4 chloromercuribenzoic acidadenine nucleotideadenosine triphosphateammoniaammonium derivativeCarboxy Lyasescarboxylyasecysteinedicarboxylic acidanimalarticlechickendialysision exchange chromatographyisolation and purificationmetabolismAdenine NucleotidesAdenosine TriphosphateAmmoniaAmmonium CompoundsAnimalCarboxy-LyasesChickensChloromercuribenzoatesChromatography, DEAE-CelluloseCysteineDialysisDicarboxylic Acids1. 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.1971info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_LlambiasBBA - Enzymology 1971;227(1):180-191reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:00Zpaperaa:paper_00052744_v227_n1_p180_LlambiasInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:01.964Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
title Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
spellingShingle Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components
Llambías, E.B.C.
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
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
dc.creator.none.fl_str_mv Llambías, E.B.C.
Del C. Batlle, A.M.
author Llambías, E.B.C.
author_facet Llambías, E.B.C.
Del C. Batlle, A.M.
author_role author
author2 Del C. Batlle, A.M.
author2_role author
dc.subject.none.fl_str_mv 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
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
dc.description.none.fl_txt_mv 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.
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.
publishDate 1971
dc.date.none.fl_str_mv 1971
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias
url http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p180_Llambias
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv BBA - Enzymology 1971;227(1):180-191
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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score 13.070432

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