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

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 treatme...

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Autores principales: Tomio, Josefina María, García, Rodolfo Carlos, San Martín de Viale, Leonor Carmen, Grinstein, Moisés
Publicado: 1970
Materias:
air
gel
pH
rat
Air
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n2_p353_Tomio
http://hdl.handle.net/20.500.12110/paper_00052744_v198_n2_p353_Tomio
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spelling paper:paper_00052744_v198_n2_p353_Tomio2023-06-08T14:29:53Z Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties Tomio, Josefina María García, Rodolfo Carlos San Martín de Viale, Leonor Carmen Grinstein, Moisés 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 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. 1970 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n2_p353_Tomio http://hdl.handle.net/20.500.12110/paper_00052744_v198_n2_p353_Tomio
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
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
spellingShingle 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
Tomio, Josefina María
García, Rodolfo Carlos
San Martín de Viale, Leonor Carmen
Grinstein, Moisés
Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
topic_facet 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
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.
author Tomio, Josefina María
García, Rodolfo Carlos
San Martín de Viale, Leonor Carmen
Grinstein, Moisés
author_facet Tomio, Josefina María
García, Rodolfo Carlos
San Martín de Viale, Leonor Carmen
Grinstein, Moisés
author_sort Tomio, Josefina María
title Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties
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
publishDate 1970
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n2_p353_Tomio
http://hdl.handle.net/20.500.12110/paper_00052744_v198_n2_p353_Tomio
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AT garciarodolfocarlos porphyrinbiosynthesisviiporphyrinogencarboxylyasefromavianerythrocytespurificationandproperties
AT sanmartindevialeleonorcarmen porphyrinbiosynthesisviiporphyrinogencarboxylyasefromavianerythrocytespurificationandproperties
AT grinsteinmoises porphyrinbiosynthesisviiporphyrinogencarboxylyasefromavianerythrocytespurificationandproperties
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