Guanine nucleotide- and GTP-dependent N6 -phenylisopropyladenosine stimulation of the membrane-bound cyclic AMP high affinity phosphodiesterase in rat brain
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منابع مشابه
Activation and phosphorylation of the 'dense-vesicle' high-affinity cyclic AMP phosphodiesterase by cyclic AMP-dependent protein kinase.
Incubation of a hepatocyte particulate fraction with ATP and the isolated catalytic unit of cyclic AMP-dependent protein kinase (A-kinase) selectively activated the high-affinity 'dense-vesicle' cycle AMP phosphodiesterase. Such activation only occurred if the membranes had been pre-treated with Mg2+. Mg2+ pre-treatment appeared to function by stimulating endogenous phosphatases and did not aff...
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Phosphorylation of the rat brain ryanodine receptor was studied using a monoclonal antibody, Ry-1, against the cardiac ryanodine receptor. A large polypeptide with the same SDS-PAGE mobility as that of the canine cardiac receptor was detected in rat brain membranes by immunoblotting. The brain ryanodine receptor was solubilized from the microsomal membranes with 3-[(3-cholamidopropyl)dimethylam...
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The kinetics of cAMP hydrolysis by the purified calf liver cGMP-stimulated cyclic nucleotide phosphodiesterase were analyzed in the absence or presence of a number of competitive inhibitors of the methylxanthine type according to a two-site competitive model for allosteric enzymes. Methylxanthines were also classified by graphical analysis of classical competition kinetics at saturating cAMP. T...
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The hormone-stimulated 'dense-vesicle' cyclic AMP phosphodiesterase was solubilized as a proteolytically 'clipped' species, and purified to apparent homogeneity from rat liver with a 2000-3000-fold purification and a 13-18% yield. It appeared to be a dimer (Mr 112,000), of two Mr-57,000 subunits. Solubilization of either a liver or a hepatocyte membrane fraction, with sodium cholate in the pres...
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Homogenate (9ml) was centrifuged at l OOOOOg (MSE Superspeed 50 centrifuge) a t 4°C for 1 h in the l o x lOml rotor. The supernatant was decanted and its volume noted. The pellet was washed twice with 5ml of buffer and was then rehomogenized in 30ml of buffer in an ice bath. Both the supernatant and rehomogenized pellet were diluted with buffer to give a range of protein concentrations. Samples...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1984
ISSN: 0014-5793
DOI: 10.1016/0014-5793(84)80849-2