Fructokinase from rat liver. I. Purification and properties

Autor:	Sánchez, J.J., González, N.S., Pontis, H.G.
Jazyk:	angličtina
Rok vydání:	1971
Předmět:	4 chloromercuribenzoic acid density gradient centrifugation Adenine Nucleotides Animal article acrylic acid derivative Absorption Acrylates Ammonium Compounds colorimetry Centrifugation Density Gradient ammonium derivative biosynthesis adenine nucleotide Chloromercuribenzoates
Zdroj:	BBA-Enzymology 1971;227(1):67-78 Biblioteca Digital (UBA-FCEN) Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN
Popis:	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.
Databáze:	OpenAIRE
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