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- W2047200063 abstract "Rabbit muscle fructose diphosphatase, purified to homogeneity, was found to require EDTA for activity at neutral, but not alkaline, pH. In the presence of EDTA the enzyme shows a single optimum at pH 7.2 with MgCl2, and two optima at pH 7.5 and 9.5 with MnCl2. The absence of the alkaline pH optimum with Mg2+ may be attributed to inhibition by this cation at alkaline pH, which is observed when the enzyme is tested in the presence of both Mn2+ and Mg2+. In addition, inhibition by excess substrate and KF is observed only in the presence of Mg2+. The concentration of EDTA required for half-maximum activity at pH 7.2 varies with the nature and concentration of the divalent cation employed. With MgCl2 (10 mm) half-maximum activity was observed with 1.5 μm EDTA; with MnCl2 (0.1 mm) the concentration of EDTA required was 0.02 mm. When the concentration of EDTA exceeded that of the divalent cation, the reaction was inhibited. Therefore, it is concluded that in addition to the absolute requirement for free Mn2+ or Mg2+, the EDTA-divalent cation complex is required for optimal activity at neutral pH. The affinity of the enzyme for EDTA-divalent cation complex is much higher with Mg2+, as compared to Mn2+. Zn2+ and Pb2+, and to a lesser extent Ca2+, were found to be strongly inhibitory; inhibition by Ca2+ was competitive with Mg2+ and Mn2+. The sensitivity to inhibition by AMP is much greater in the presence of Mg2+, as compared with Mn2+. The results suggest that the conformations induced by Mg2+ and Mn2+ are different, with the former being more sensitive to effectors than the conformation induced by Mn2+." @default.
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- W2047200063 date "1972-08-01" @default.
- W2047200063 modified "2023-10-12" @default.
- W2047200063 title "Activation of rabbit muscle fructose diphosphatase by EDTA and the effect of divalent cations" @default.
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- W2047200063 doi "https://doi.org/10.1016/0003-9861(72)90536-x" @default.
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