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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00052744_v198_n2_p353_Tomio
Ver los metadatos del registro completo
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paperaa:paper_00052744_v198_n2_p353_Tomio |
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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/ar2025-09-29T13:42:50Zpaperaa: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:18962025-09-29 13:42:50.857Biblioteca 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_ |
1844618733289472000 |
score |
13.070432 |