Separate Phosphodiesterases for the Hydrolysis of Cyclic Adenosine 3',5'-Monophosphate and Cyclic Guanosine 3',5'-Monophosphate in Rat Liver
作者： T.R. Russell , W.L. Terasaki , M.M. Appleman
DOI: 10.1016/S0021-9258(19)44303-2
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摘要: Abstract Rat liver contains at least three active cyclic nucleotide phosphodiesterase fractions which differ in their substrate affinity, specificity, and subcellular distribution. These forms have been separated by DEAE-cellulose chromatography. Fraction I hydrolyzes guanosine 3',5'-monophosphate (cyclic GMP), this activity is unaffected adenosine AMP). This enzyme shows linear kinetics with a high affinity for GMP. II both nucleotides relatively low affinities similar to those observed kinetically the original homogenate. Each acts as noncompetitive inhibitor of hydrolysis other nucleotide. However, GMP concentrations (1 µm) an activator AMP hydrolysis. Cooperativity seen pH 7.4 but not 8.0. III negatively cooperative inhibited hyperbolic fashion. associated 100,000 x g particles, while Fractions are soluble.
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