Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase

D. W. Meek, H. G. Nimmo

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    25 Citations (Scopus)


    A new purification procedure for rat liver fructose-1,6-bisphosphatase that involves use of Procion Red-Sepharose is described. The purified enzyme was homogeneous, had a subunit Mr of 40 000-41 000 and seemed to be undegraded. The enzyme could be phosphorylated by cyclic AMP-dependent protein kinase with a stoicheiometry of one per subunit. Phosphorylation caused a 2-fold decrease in the Km of the enzyme for fructose 1,6-bisphosphate, but did not affect its allosteric responses to AMP, Mg2+ and fructose 2,6-bisphosphate.
    Original languageEnglish
    Pages (from-to)125-130
    Number of pages6
    JournalBiochemical Journal
    Issue number1
    Publication statusPublished - 15 Aug 1984


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