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- W2077453236 abstract "A new procedure for the purification of rabbit kidney fructose 1,6-diphosphatase yields an enzyme with optimum activity at pH 7.0–7.5, in contrast to the alkaline pH optimum observed with earlier preparations. The purified enzyme hydrolyzes fructose-1,6-P2 and sedoheptulose-1,7-P2 at approximately equal rates, although the affinity for the former is much higher, and the pH optima are somewhat different. Homogeneity of the enzyme preparation was established by disc gel electrophoresis and ultracentrifugal analysis; the latter indicates the presence of a single protein of molecular weight of 140,000. The molecular weight of the subunits dissociated by treatment with maleic anhydride was found to be 37,500. The amino acid composition was similar to that reported previously for the enzyme with alkaline pH optimum, but several amino acids were present in significantly greater amounts. The enzyme was very sensitive to inhibition by AMP, and was also inhibited by high concentrations of fructose-1,6-P2." @default.
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- W2077453236 date "1972-03-01" @default.
- W2077453236 modified "2023-10-12" @default.
- W2077453236 title "Purification and properties of a rabbit kidney fructose diphosphatase with neutral pH optimum" @default.
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- W2077453236 doi "https://doi.org/10.1016/0003-9861(72)90305-0" @default.
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