Fructokinase from rat liver. I. Purification and properties

En:

BBA - Enzymology 1971;227(1):67-78

Fecha:

1971

Formato:

application/pdf

Tipo de documento:

info:eu-repo/semantics/article
info:ar-repo/semantics/artículo
info:eu-repo/semantics/publishedVersion

Idioma:

eng

Descriptores:

4 chloromercuribenzoic acid -  acrylic acid derivative -  adenine nucleotide -  ammonium derivative -  absorption -  animal -  article -  biosynthesis -  colorimetry

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.

Identificador(es):

http://hdl.handle.net/20.500.12110/paper_00052744_v227_n1_p67_Sanchez

Derechos:

info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar