Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties

Autores
Tomio, J.M.; García, R.C.; San Martín De Viale, L.C.; Grinstein, M.
Año de publicación
1970
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. 2. 2. The purified material appears to be homogeneous in polyacrylamide gel disc electrophoresis. 3. 3. The enzyme was heat labile and inhibited by sodium salt; the activity was enhanced by EDTA, GSH and boiled rat-liver extract. 4. 4. The influence of these chemical and physical agents on the removal of the first and second carboxyl groups from uroporphyrinogen was compared; the second group was more susceptible to these agents. 5. 5. The possibility that one or several enzymes were involved in the stepwise decarboxylation of uroporphyrinogen is discussed. 6. 6. The general name of porphyrinogen carboxy-lyase for the enzyme system is proposed because of the different porphyrinogens it can decarboxylate. © 1970.
Fil:Tomio, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:García, R.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:San Martín De Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
BBA - Enzymology 1970;198(2):353-363
Materia
acrylic acid derivative
ammonium derivative
Carboxy Lyases
carboxylyase
cellulose
edetic acid
glutathione
porphyrin
sodium
sulfate
air
animal
article
chicken
drug stability
enzyme activation
enzymology
erythrocyte
gel
gel electrophoresis
heat
ion exchange chromatography
isolation and purification
liver
pH
precipitation
rat
technique
Acrylates
Air
Ammonium Compounds
Animal
Carboxy-Lyases
Cellulose
Chickens
Chromatography, DEAE-Cellulose
Drug Stability
Edetic Acid
Electrophoresis, Disc
Enzyme Activation
Erythrocytes
Gels
Glutathione
Heat
Hydrogen-Ion Concentration
Liver
Methods
Porphyrins
Precipitation
Rats
Sodium
Sulfates
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_v198_n2_p353_Tomio
Acceder
id BDUBAFCEN_f8f8e1af89251bbf8b1af3f5ceb3feeb
oai_identifier_str paperaa:paper_00052744_v198_n2_p353_Tomio
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and propertiesTomio, J.M.García, R.C.San Martín De Viale, L.C.Grinstein, M.acrylic acid derivativeammonium derivativeCarboxy Lyasescarboxylyasecelluloseedetic acidglutathioneporphyrinsodiumsulfateairanimalarticlechickendrug stabilityenzyme activationenzymologyerythrocytegelgel electrophoresisheation exchange chromatographyisolation and purificationliverpHprecipitationrattechniqueAcrylatesAirAmmonium CompoundsAnimalCarboxy-LyasesCelluloseChickensChromatography, DEAE-CelluloseDrug StabilityEdetic AcidElectrophoresis, DiscEnzyme ActivationErythrocytesGelsGlutathioneHeatHydrogen-Ion ConcentrationLiverMethodsPorphyrinsPrecipitationRatsSodiumSulfates1. 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. 2. 2. The purified material appears to be homogeneous in polyacrylamide gel disc electrophoresis. 3. 3. The enzyme was heat labile and inhibited by sodium salt; the activity was enhanced by EDTA, GSH and boiled rat-liver extract. 4. 4. The influence of these chemical and physical agents on the removal of the first and second carboxyl groups from uroporphyrinogen was compared; the second group was more susceptible to these agents. 5. 5. The possibility that one or several enzymes were involved in the stepwise decarboxylation of uroporphyrinogen is discussed. 6. 6. The general name of porphyrinogen carboxy-lyase for the enzyme system is proposed because of the different porphyrinogens it can decarboxylate. © 1970.Fil:Tomio, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:García, R.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:San Martín De Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1970info: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_v198_n2_p353_TomioBBA - Enzymology 1970;198(2):353-363reponame: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/ar2025-10-23T11:18:12Zpaperaa:paper_00052744_v198_n2_p353_TomioInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:13.737Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
title Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
spellingShingle Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
Tomio, J.M.
acrylic acid derivative
ammonium derivative
Carboxy Lyases
carboxylyase
cellulose
edetic acid
glutathione
porphyrin
sodium
sulfate
air
animal
article
chicken
drug stability
enzyme activation
enzymology
erythrocyte
gel
gel electrophoresis
heat
ion exchange chromatography
isolation and purification
liver
pH
precipitation
rat
technique
Acrylates
Air
Ammonium Compounds
Animal
Carboxy-Lyases
Cellulose
Chickens
Chromatography, DEAE-Cellulose
Drug Stability
Edetic Acid
Electrophoresis, Disc
Enzyme Activation
Erythrocytes
Gels
Glutathione
Heat
Hydrogen-Ion Concentration
Liver
Methods
Porphyrins
Precipitation
Rats
Sodium
Sulfates
title_short Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
title_full Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
title_fullStr Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
title_full_unstemmed Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
title_sort Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
dc.creator.none.fl_str_mv Tomio, J.M.
García, R.C.
San Martín De Viale, L.C.
Grinstein, M.
author Tomio, J.M.
author_facet Tomio, J.M.
García, R.C.
San Martín De Viale, L.C.
Grinstein, M.
author_role author
author2 García, R.C.
San Martín De Viale, L.C.
Grinstein, M.
author2_role author
author
author
dc.subject.none.fl_str_mv acrylic acid derivative
ammonium derivative
Carboxy Lyases
carboxylyase
cellulose
edetic acid
glutathione
porphyrin
sodium
sulfate
air
animal
article
chicken
drug stability
enzyme activation
enzymology
erythrocyte
gel
gel electrophoresis
heat
ion exchange chromatography
isolation and purification
liver
pH
precipitation
rat
technique
Acrylates
Air
Ammonium Compounds
Animal
Carboxy-Lyases
Cellulose
Chickens
Chromatography, DEAE-Cellulose
Drug Stability
Edetic Acid
Electrophoresis, Disc
Enzyme Activation
Erythrocytes
Gels
Glutathione
Heat
Hydrogen-Ion Concentration
Liver
Methods
Porphyrins
Precipitation
Rats
Sodium
Sulfates
topic acrylic acid derivative
ammonium derivative
Carboxy Lyases
carboxylyase
cellulose
edetic acid
glutathione
porphyrin
sodium
sulfate
air
animal
article
chicken
drug stability
enzyme activation
enzymology
erythrocyte
gel
gel electrophoresis
heat
ion exchange chromatography
isolation and purification
liver
pH
precipitation
rat
technique
Acrylates
Air
Ammonium Compounds
Animal
Carboxy-Lyases
Cellulose
Chickens
Chromatography, DEAE-Cellulose
Drug Stability
Edetic Acid
Electrophoresis, Disc
Enzyme Activation
Erythrocytes
Gels
Glutathione
Heat
Hydrogen-Ion Concentration
Liver
Methods
Porphyrins
Precipitation
Rats
Sodium
Sulfates
dc.description.none.fl_txt_mv 1. 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. 2. 2. The purified material appears to be homogeneous in polyacrylamide gel disc electrophoresis. 3. 3. The enzyme was heat labile and inhibited by sodium salt; the activity was enhanced by EDTA, GSH and boiled rat-liver extract. 4. 4. The influence of these chemical and physical agents on the removal of the first and second carboxyl groups from uroporphyrinogen was compared; the second group was more susceptible to these agents. 5. 5. The possibility that one or several enzymes were involved in the stepwise decarboxylation of uroporphyrinogen is discussed. 6. 6. The general name of porphyrinogen carboxy-lyase for the enzyme system is proposed because of the different porphyrinogens it can decarboxylate. © 1970.
Fil:Tomio, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:García, R.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:San Martín De Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. 2. 2. The purified material appears to be homogeneous in polyacrylamide gel disc electrophoresis. 3. 3. The enzyme was heat labile and inhibited by sodium salt; the activity was enhanced by EDTA, GSH and boiled rat-liver extract. 4. 4. The influence of these chemical and physical agents on the removal of the first and second carboxyl groups from uroporphyrinogen was compared; the second group was more susceptible to these agents. 5. 5. The possibility that one or several enzymes were involved in the stepwise decarboxylation of uroporphyrinogen is discussed. 6. 6. The general name of porphyrinogen carboxy-lyase for the enzyme system is proposed because of the different porphyrinogens it can decarboxylate. © 1970.
publishDate 1970
dc.date.none.fl_str_mv 1970
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_v198_n2_p353_Tomio
url http://hdl.handle.net/20.500.12110/paper_00052744_v198_n2_p353_Tomio
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 1970;198(2):353-363
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
_version_ 1846784875390042112
score 12.982451

Publicaciones similares