Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies

Autores
Llambías, E.B.C.; Del C. Batlle, A.M.
Año de publicación
1970
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 1970.
Fil:Llambías, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
BBA - Enzymology 1970;220(3):552-559
Materia
ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
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_v220_n3_p552_Llambias
Acceder
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oai_identifier_str paperaa:paper_00052744_v220_n3_p552_Llambias
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studiesLlambías, E.B.C.Del C. Batlle, A.M.ammonium derivativearticlebinding siteAmmonium CompoundsBinding SitesKinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 1970.Fil:Llambías, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Del C. Batlle, A.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_v220_n3_p552_LlambiasBBA - Enzymology 1970;220(3):552-559reponame: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/ar2025-09-29T13:43:09Zpaperaa:paper_00052744_v220_n3_p552_LlambiasInstitucionalhttps://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 13:43:10.763Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
title Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
spellingShingle Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
Llambías, E.B.C.
ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
title_short Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
title_full Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
title_fullStr Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
title_full_unstemmed Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
title_sort Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
dc.creator.none.fl_str_mv Llambías, E.B.C.
Del C. Batlle, A.M.
author Llambías, E.B.C.
author_facet Llambías, E.B.C.
Del C. Batlle, A.M.
author_role author
author2 Del C. Batlle, A.M.
author2_role author
dc.subject.none.fl_str_mv ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
topic ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
dc.description.none.fl_txt_mv Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 1970.
Fil:Llambías, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Kinetic studies were carried out using purified porphobilinogenase and deaminase preparations in the presence and absence of ammonium ions. It has been found in plots of v versus [S] that a deviation from the Michaelis-Menten hyperbola occurs with both enzymes; double-reciprocal plots were concave downward; Rs values were greater than 81; and in some cases the Hill coefficient was less than 1, indicating negative homotropic kinetics. Evidence also suggested that porphobilinogenase contains at least two substrate-binding sites per molecule of enzyme. It has also been found that ammonium ions act competitively on the first reaction of the porphobilinogenase. © 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_v220_n3_p552_Llambias
url http://hdl.handle.net/20.500.12110/paper_00052744_v220_n3_p552_Llambias
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;220(3):552-559
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
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score 13.070432

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