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- W2018375018 abstract "Abstract The rate of cyclic AMP formation by rabbit heart membrane particles decreased at assay temperatures greater than 30 °C. Adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] activity (assayed at 24 °C) decreased exponentially with time of preincubation at 30 or 37 °C, providing evidence for the instability of this enzyme. The half-life, t1/2, of the enzyme at 37 °C was 9.9 min in the absence and 4.4 min in the presence of MgCl2. The activity was most labile in the presence of 50 m m Mg2+ and 1 m m ATP, having t1/2 = 1.3min. Prior incubation of membranes with the GTP analog, guanyl-5′-yl imidodiphosphate [Gpp(NH)p], 0.1 m m , for 30 min at 37 °C produced maximal activation of adenylate cyclase; the rate of activation was temperature dependent and was increased in the presence of isoproterenol. The Gpp(NH)p-activated enzyme had increased thermal stability, t1/2 = 170 min, and was also markedly more stable in the presence of Mg-ATP, t1/2 = 72min, than nonactivated enzyme. Preactivation with F− (30 min at 24 °C) also stabilized the activity; t1/2 > 70 min in the absence or presence of Mg-ATP. The Mg2+ concentration required for maximal activity was reduced from approximately 60 m m for nonactivated enzyme to 10 m m for the Gpp(NH)p- and F−activated enzyme." @default.
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- W2018375018 modified "2023-09-23" @default.
- W2018375018 title "Activation and stabilization of cardiac adenylate cyclase by GTP analog and fluoride" @default.
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- W2018375018 doi "https://doi.org/10.1016/0003-9861(78)90150-9" @default.
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