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- W2077955338 abstract "Glycogen phosphorylases a, ab and b, purified from locust flight muscle, are characterized with respect to pH effect, substrate affinity and AMP dependency. pH optima of the three enzyme forms, measured in the absence and presence of AMP, range between 6.9 and 7.2. Michaelis constants (Km) are 0.5 mM glycogen, 1.15 mM Pi and 0.03 μM AMP for phosphorylase a; 0.5 mM glycogen, 2.6 mM Pi and 7 μM AMP for phosphorylase ab; 0.1 mM glycogen, 20 mM Pi and approx. 270 μM AMP for phosphorylase b. For all three forms the Km are enhanced, in a concentration-dependent way, by nonsaturating concentrations of cosubstrate and/or AMP, conditions which decrease the apparent maximal velocity (Vmax). Enzyme activity is decreased by AMP concentrations exceeding 2 mM (phosphorylase a) or 5 mM (phosphorylase ab and b). ATP inhibits competitively the AMP-dependent activation of phosphorylase b, with a Ki of 270 μM in the presence of 2 mM AMP, without affecting the Vmax. ATP also increases the apparent Km for both substrates. ATP has no effect on the kinetic parameters of phosphorylase a and ab. Results are discussed in relation to a possible regulation of phosphorylase activity in vivo by metabolic effectors (substrates, AMP, ATP), both in locusts at rest and after flight." @default.
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- W2077955338 date "1987-01-01" @default.
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- W2077955338 title "Kinetic properties of glycogen phosphorylases and from flight muscles of the locust, Locusta migratoria" @default.
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- W2077955338 doi "https://doi.org/10.1016/0020-1790(87)90038-2" @default.
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