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
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00052744_v191_n1_p130_Sancovich
Acceder
id BDUBAFCEN_270ae98327136ed59960a804f40cc868
oai_identifier_str paperaa:paper_00052744_v191_n1_p130_Sancovich
network_acronym_str BDUBAFCEN
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/ar2025-10-23T11:18:15Zpaperaa: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:18962025-10-23 11:18:16.853Biblioteca 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_ 1846784876138725376
score 12.982451

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