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- W2018736006 abstract "Optimal conditions for assaying and stabilizing the soluble cGMP-binding activity in Dictyostelium discoideum were established. Using these procedures, we investigated the relationship between the cGMP-binding activity and the cGMP-specific phosphodiesterase in this organism. In wild-type strains, the binding and phosphodiesterase activities were found to be regulated differently during development. Also, stmF mutants, which possess very low levels of cGMP-specific phosphodiesterase activity, exhibited normal levels of cGMP-binding activity. Fractionation studies revealed that the binding and phosphodiesterase activities could be resolved by DEAE-cellulose chromatography. Finally, the effect of pH on cGMP binding was different from that reported for cGMP-mediated activation of the phosphodiesterase. Taken together, these results indicate that the cGMP-binding protein and the cGMP-specific phosphodiesterase are probably unrelated. In addition, the cGMP-binding activity is not associated with cGMP-stimulated kinase activity and it does not elute from DEAE-cellulose like the highly conserved cGMP-dependent protein kinases found in other systems." @default.
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- W2018736006 date "1986-06-01" @default.
- W2018736006 modified "2023-09-23" @default.
- W2018736006 title "Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in <i>Dictyostelium discoideum</i>" @default.
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- W2018736006 doi "https://doi.org/10.1139/o86-074" @default.
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