Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme
- Autores
- Sancovich, H.A.; Batlle, A.M.C.; Grinstein, M.
- Año de publicación
- 1969
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969.
Fil:Sancovich, H.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Batlle, A.M.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 1969;191(1):130-143
- Materia
-
ammonium derivative
isomerase
lyase
porphyrin
pyrrole derivative
animal
article
binding site
biosynthesis
cattle
dialysis
enzyme activation
enzymology
filtration
gel chromatography
isolation and purification
kinetics
liver
pH
precipitation
technique
temperature
Ammonium Compounds
Animal
Binding Sites
Cattle
Chromatography, Gel
Dialysis
Enzyme Activation
Filtration
Hydrogen-Ion Concentration
Isomerases
Kinetics
Liver
Lyases
Methods
Porphyrins
Precipitation
Pyrroles
Temperature - 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_v191_n1_p130_Sancovich
Ver los metadatos del registro completo
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paperaa:paper_00052744_v191_n1_p130_Sancovich |
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repository_id_str |
1896 |
network_name_str |
Biblioteca Digital (UBA-FCEN) |
spelling |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzymeSancovich, H.A.Batlle, A.M.C.Grinstein, M.ammonium derivativeisomeraselyaseporphyrinpyrrole derivativeanimalarticlebinding sitebiosynthesiscattledialysisenzyme activationenzymologyfiltrationgel chromatographyisolation and purificationkineticsliverpHprecipitationtechniquetemperatureAmmonium CompoundsAnimalBinding SitesCattleChromatography, GelDialysisEnzyme ActivationFiltrationHydrogen-Ion ConcentrationIsomerasesKineticsLiverLyasesMethodsPorphyrinsPrecipitationPyrrolesTemperature1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969.Fil:Sancovich, H.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Batlle, A.M.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.1969info: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_v191_n1_p130_SancovichBBA - Enzymology 1969;191(1):130-143reponame: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/ar2025-09-29T13:42:52Zpaperaa:paper_00052744_v191_n1_p130_SancovichInstitucionalhttps://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 13:42:53.316Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
title |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
spellingShingle |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme Sancovich, H.A. ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature |
title_short |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
title_full |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
title_fullStr |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
title_full_unstemmed |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
title_sort |
Porphyrin biosynthesis. VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver. Porphobilinogenase an allosteric enzyme |
dc.creator.none.fl_str_mv |
Sancovich, H.A. Batlle, A.M.C. Grinstein, M. |
author |
Sancovich, H.A. |
author_facet |
Sancovich, H.A. Batlle, A.M.C. Grinstein, M. |
author_role |
author |
author2 |
Batlle, A.M.C. Grinstein, M. |
author2_role |
author author |
dc.subject.none.fl_str_mv |
ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature |
topic |
ammonium derivative isomerase lyase porphyrin pyrrole derivative animal article binding site biosynthesis cattle dialysis enzyme activation enzymology filtration gel chromatography isolation and purification kinetics liver pH precipitation technique temperature Ammonium Compounds Animal Binding Sites Cattle Chromatography, Gel Dialysis Enzyme Activation Filtration Hydrogen-Ion Concentration Isomerases Kinetics Liver Lyases Methods Porphyrins Precipitation Pyrroles Temperature |
dc.description.none.fl_txt_mv |
1. 1.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969. Fil:Sancovich, H.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A.M.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.|Porphobilinogenase has been isolated and purified from cow liver and its components, porphobilinogen deaminase and uroporphyrinogen isomerase, have been separated from each other and purified. 2. 2.|The effect of NH4+ was studied. The deaminase exhibited classical Michaelis-Menten kinetics in the absence or presence of NH4+, which at high concentrations behaved as a noncompetitive inhibitor of the deaminase. As expected from Hill plots, n = 1 both in the absence or presence of NH4+. Instead, when activity of porpho bilinogenase is plotted versus porphobilinogen concentration, sigmoid curves are obtained; but the presence of NH4+ at different concentrations altered the kinetic parameters of this enzymic system, again showing normal kinetics. In addition, n values were found to be 2 for porphobilinogen per porphobilinogenase molecule and 1 in the presence of NH4+ which behaves as a competitive inhibitor of the isomerase. Results are discussed in relation to the allosteric theories of monod et al.1,2 and liver porphobilinogenase is proposed to be an allosteric protein. 3. 3.|The presence of an ultrafiltrable factor which stimulates uroporphyrinogen formation from porphobilinogen has been revealed. © 1969. |
publishDate |
1969 |
dc.date.none.fl_str_mv |
1969 |
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_v191_n1_p130_Sancovich |
url |
http://hdl.handle.net/20.500.12110/paper_00052744_v191_n1_p130_Sancovich |
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 1969;191(1):130-143 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_ |
1844618734051786752 |
score |
13.070432 |