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- W2000892287 abstract "Abstract Acid phosphatase purified from maize scutellum, upon acylation with succinic anhydride, still shows negative co-operativity for the hydrolysis of glucose-6-phosphate at pH 5.4. This phenomenon is abolished by glucose, for both native and succinylated enzymes, through stimulation of the initial velocities at sub-optimal substrate concentrations. However, negative co-operativity for the enzymatic hydrolysis of p -nitrophenylphosphate at pH 5.4 is suppressed only at high concentrations of glucose. Furthermore, the hydrolysis of p -nitrophenylphosphate is noncompetitively inhibited (low affinity form of the enzyme molecule) by glucose, which suggests the existence of different substrate binding sites." @default.
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- W2000892287 date "1983-01-01" @default.
- W2000892287 modified "2023-09-23" @default.
- W2000892287 title "Acid phosphatase from maize scutellum: Negative cooperativity suppression by glucose" @default.
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- W2000892287 doi "https://doi.org/10.1016/0031-9422(83)80008-9" @default.
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