Fructokinase from rat liver. I. Purification and properties

Autores
Sánchez, J.J.; González, N.S.; Pontis, H.G.
Año de publicación
1971
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fructokinase (ATP:d-fructose-1-phosphate transferase, EC 2.7.1.3) from rat liver has been purified 400-fold. The purification procedure involves an acid treatment, a heat step at 65°, (NH4)2SO4 fractionation, chromatography on Sephadex G-100 and finally (NH4)2SO4 extraction. The enzyme appears nearly homogenous by density gradient centrifugation but gives a single peak in sedimentation velocity analysis. Purified liver fructokinase has a Km of 0.46-0.80 mM for fructose and 1.56-1.33 mM for MgATP at a K+ concentration of 0.4 and 0.1 M, respectively. The enzyme also phosphorylates l-sorbose and d-tagatose. No difference could be found in the phosphorylation of the pyranose and furanose forms of fructose. The enzyme is inhibited by p-chloromercuribenzoate and is stable up to 50-55°. © 1971.
Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pontis, H.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
BBA - Enzymology 1971;227(1):67-78
Materia
4 chloromercuribenzoic acid
acrylic acid derivative
adenine nucleotide
ammonium derivative
absorption
animal
article
biosynthesis
colorimetry
density gradient centrifugation
Absorption
Acrylates
Adenine Nucleotides
Ammonium Compounds
Animal
Centrifugation, Density Gradient
Chloromercuribenzoates
Colorimetry
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_v227_n1_p67_Sanchez
Acceder
id BDUBAFCEN_65dfae7bbb167f17a4fb7fe4609232bf
oai_identifier_str paperaa:paper_00052744_v227_n1_p67_Sanchez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Fructokinase from rat liver. I. Purification and propertiesSánchez, J.J.González, N.S.Pontis, H.G.4 chloromercuribenzoic acidacrylic acid derivativeadenine nucleotideammonium derivativeabsorptionanimalarticlebiosynthesiscolorimetrydensity gradient centrifugationAbsorptionAcrylatesAdenine NucleotidesAmmonium CompoundsAnimalCentrifugation, Density GradientChloromercuribenzoatesColorimetryFructokinase (ATP:d-fructose-1-phosphate transferase, EC 2.7.1.3) from rat liver has been purified 400-fold. The purification procedure involves an acid treatment, a heat step at 65°, (NH4)2SO4 fractionation, chromatography on Sephadex G-100 and finally (NH4)2SO4 extraction. The enzyme appears nearly homogenous by density gradient centrifugation but gives a single peak in sedimentation velocity analysis. Purified liver fructokinase has a Km of 0.46-0.80 mM for fructose and 1.56-1.33 mM for MgATP at a K+ concentration of 0.4 and 0.1 M, respectively. The enzyme also phosphorylates l-sorbose and d-tagatose. No difference could be found in the phosphorylation of the pyranose and furanose forms of fructose. The enzyme is inhibited by p-chloromercuribenzoate and is stable up to 50-55°. © 1971.Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Pontis, H.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1971info: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_v227_n1_p67_SanchezBBA - Enzymology 1971;227(1):67-78reponame: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/ar2025-09-29T13:43:01Zpaperaa:paper_00052744_v227_n1_p67_SanchezInstitucionalhttps://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 13:43:02.05Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Fructokinase from rat liver. I. Purification and properties
title Fructokinase from rat liver. I. Purification and properties
spellingShingle Fructokinase from rat liver. I. Purification and properties
Sánchez, J.J.
4 chloromercuribenzoic acid
acrylic acid derivative
adenine nucleotide
ammonium derivative
absorption
animal
article
biosynthesis
colorimetry
density gradient centrifugation
Absorption
Acrylates
Adenine Nucleotides
Ammonium Compounds
Animal
Centrifugation, Density Gradient
Chloromercuribenzoates
Colorimetry
title_short Fructokinase from rat liver. I. Purification and properties
title_full Fructokinase from rat liver. I. Purification and properties
title_fullStr Fructokinase from rat liver. I. Purification and properties
title_full_unstemmed Fructokinase from rat liver. I. Purification and properties
title_sort Fructokinase from rat liver. I. Purification and properties
dc.creator.none.fl_str_mv Sánchez, J.J.
González, N.S.
Pontis, H.G.
author Sánchez, J.J.
author_facet Sánchez, J.J.
González, N.S.
Pontis, H.G.
author_role author
author2 González, N.S.
Pontis, H.G.
author2_role author
author
dc.subject.none.fl_str_mv 4 chloromercuribenzoic acid
acrylic acid derivative
adenine nucleotide
ammonium derivative
absorption
animal
article
biosynthesis
colorimetry
density gradient centrifugation
Absorption
Acrylates
Adenine Nucleotides
Ammonium Compounds
Animal
Centrifugation, Density Gradient
Chloromercuribenzoates
Colorimetry
topic 4 chloromercuribenzoic acid
acrylic acid derivative
adenine nucleotide
ammonium derivative
absorption
animal
article
biosynthesis
colorimetry
density gradient centrifugation
Absorption
Acrylates
Adenine Nucleotides
Ammonium Compounds
Animal
Centrifugation, Density Gradient
Chloromercuribenzoates
Colorimetry
dc.description.none.fl_txt_mv Fructokinase (ATP:d-fructose-1-phosphate transferase, EC 2.7.1.3) from rat liver has been purified 400-fold. The purification procedure involves an acid treatment, a heat step at 65°, (NH4)2SO4 fractionation, chromatography on Sephadex G-100 and finally (NH4)2SO4 extraction. The enzyme appears nearly homogenous by density gradient centrifugation but gives a single peak in sedimentation velocity analysis. Purified liver fructokinase has a Km of 0.46-0.80 mM for fructose and 1.56-1.33 mM for MgATP at a K+ concentration of 0.4 and 0.1 M, respectively. The enzyme also phosphorylates l-sorbose and d-tagatose. No difference could be found in the phosphorylation of the pyranose and furanose forms of fructose. The enzyme is inhibited by p-chloromercuribenzoate and is stable up to 50-55°. © 1971.
Fil:González, N.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pontis, H.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Fructokinase (ATP:d-fructose-1-phosphate transferase, EC 2.7.1.3) from rat liver has been purified 400-fold. The purification procedure involves an acid treatment, a heat step at 65°, (NH4)2SO4 fractionation, chromatography on Sephadex G-100 and finally (NH4)2SO4 extraction. The enzyme appears nearly homogenous by density gradient centrifugation but gives a single peak in sedimentation velocity analysis. Purified liver fructokinase has a Km of 0.46-0.80 mM for fructose and 1.56-1.33 mM for MgATP at a K+ concentration of 0.4 and 0.1 M, respectively. The enzyme also phosphorylates l-sorbose and d-tagatose. No difference could be found in the phosphorylation of the pyranose and furanose forms of fructose. The enzyme is inhibited by p-chloromercuribenzoate and is stable up to 50-55°. © 1971.
publishDate 1971
dc.date.none.fl_str_mv 1971
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_v227_n1_p67_Sanchez
url http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p67_Sanchez
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 1971;227(1):67-78
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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