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Two forms of 6‐phosphofructo‐2‐kinase have been identified in Saccharomyces cerevisiae by their different chromatographic behaviour on CM‐Sephadex C‐50. One of them was not adsorbed and represented ∼ 30% of the eluted activity. The other one emerged at about 120 mM KCl. A molecular mass of 120 kDa was found for both of them. No differences in kinetic behaviour in susceptibility to activation by cAMP‐dependent protein kinase were found between the two forms.
Enzyme Activation, Isoenzymes, Kinetics, Fructose 2,6-bisphosphate, (Yeast), Phosphofructokinase-1, 6-Phosphofructo-2-kinase, Saccharomyces cerevisiae, Protein Kinases
Enzyme Activation, Isoenzymes, Kinetics, Fructose 2,6-bisphosphate, (Yeast), Phosphofructokinase-1, 6-Phosphofructo-2-kinase, Saccharomyces cerevisiae, Protein Kinases
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