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- W2018269413 abstract "(1) The active form of rabbit liver phosphofructokinase when preincubated in presence of F− and effectors of the enzyme is stabilized against its conversion to less active form as a result of dilution. (2) The stabilized active form of enzyme has a Km value of 0.01 mM for fructose 6-phosphate, the same as measured in presence of all the positive effectors, and is lower, by 13 times, than the Km value of the non-stabilized control enzyme, and exhibits normal Michaelis-Menten kinetics, in contrast to the non-stabilized control enzyme which shows sigmoidal kinetics. (3) The stabilized active form of enzyme is neither inhibited by excess concentration of ATP nor activated by activators of phosphofructokinase. (4) The data thus support the proposition that the enzyme does indeed exist in two interconvertible forms with enormous difference in their affinities for fructose 6-phosphate and effectors." @default.
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- W2018269413 date "1974-04-01" @default.
- W2018269413 modified "2023-10-16" @default.
- W2018269413 title "Stabilization of active form of rabbit liver phosphofructokinase" @default.
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- W2018269413 doi "https://doi.org/10.1016/0006-291x(74)90613-5" @default.
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