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- W2090647065 abstract "1. Pyruvate kinase from the plerocercoid of Ligula intestinalis has an optimum pH of 7.0 and a high affinity for Mn2+. 2. A plot of the change in reaction rate with increasing phosphoenolpyruvate concentration gives a sigmoid curve which is transformed into a Michaelis-Menten relationship in the presence of fructose 1,6-diphosphate. 3. ATP and malate inhibit activity in a cooperative manner. 4. The results suggest that changes in the intracellular levels of phosphoenolpyruvate, ATP, malate, fructose 1,6-diphosphate and H+ control the activity of pyruvate kinase in vivo." @default.
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- W2090647065 date "1975-02-01" @default.
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- W2090647065 title "Pyruvate kinase in the plerocercoid of Ligula intestinalis (Cestoda: Pseudophyllidea)" @default.
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- W2090647065 doi "https://doi.org/10.1016/0020-711x(75)90108-1" @default.
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