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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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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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 |
_version_ |
1768544892468854784 |