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

Mostrar todas las versiones(3)

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 plot...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Llambías, E.B.C., Del C. Batlle, A.M.
Formato: Artículo publishedVersion
Publicado: 1970
Materias:
ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v220_n3_p552_Llambias
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v220_n3_p552_Llambias_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
id I28-R145-paper_00052744_v220_n3_p552_Llambias_oai
record_format dspace
spelling I28-R145-paper_00052744_v220_n3_p552_Llambias_oai2024-08-16 Llambías, E.B.C. Del C. Batlle, A.M. 1970 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. application/pdf http://hdl.handle.net/20.500.12110/paper_00052744_v220_n3_p552_Llambias info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar BBA - Enzymology 1970;220(3):552-559 ammonium derivative article binding site Ammonium Compounds Binding Sites Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v220_n3_p552_Llambias_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
spellingShingle ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
Llambías, E.B.C.
Del C. Batlle, A.M.
Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
topic_facet ammonium derivative
article
binding site
Ammonium Compounds
Binding Sites
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.
format Artículo
Artículo
publishedVersion
author Llambías, E.B.C.
Del C. Batlle, A.M.
author_facet Llambías, E.B.C.
Del C. Batlle, A.M.
author_sort Llambías, E.B.C.
title Porphyrin biosynthesis in soybean callus. V. The porphobilinogen deaminase-uroporphyrinogen cosynthetase system. Kinetic studies
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
publishDate 1970
url http://hdl.handle.net/20.500.12110/paper_00052744_v220_n3_p552_Llambias
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v220_n3_p552_Llambias_oai
work_keys_str_mv AT llambiasebc porphyrinbiosynthesisinsoybeancallusvtheporphobilinogendeaminaseuroporphyrinogencosynthetasesystemkineticstudies
AT delcbatlleam porphyrinbiosynthesisinsoybeancallusvtheporphobilinogendeaminaseuroporphyrinogencosynthetasesystemkineticstudies
_version_ 1809356953606946816

Ejemplares similares