Fructokinase from rat liver. I. Purification and properties

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 nearl...

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Autores principales: González, Nélida Susana, Pontis Videla, Horacio G.
Publicado: 1971
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p67_Sanchez
http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p67_Sanchez
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spelling paper:paper_00052744_v227_n1_p67_Sanchez2023-06-08T14:29:55Z Fructokinase from rat liver. I. Purification and properties González, Nélida Susana Pontis Videla, Horacio G. 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 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. 1971 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p67_Sanchez http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p67_Sanchez
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
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
spellingShingle 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
González, Nélida Susana
Pontis Videla, Horacio G.
Fructokinase from rat liver. I. Purification and properties
topic_facet 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
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.
author González, Nélida Susana
Pontis Videla, Horacio G.
author_facet González, Nélida Susana
Pontis Videla, Horacio G.
author_sort González, Nélida Susana
title Fructokinase from rat liver. I. Purification and properties
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
publishDate 1971
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v227_n1_p67_Sanchez
http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p67_Sanchez
work_keys_str_mv AT gonzaleznelidasusana fructokinasefromratliveripurificationandproperties
AT pontisvidelahoraciog fructokinasefromratliveripurificationandproperties
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