Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation
Crude preparations of cyclic adenosine 3′, 5′-monophosphate phosphodiesterase were activated 1.5 to 2 fold by incubation with ATP, Mg2+ and cyclic AMP in a reaction which was both, time and temperature dependent. Cyclic AMP phosphodiesterase remained in an activated state upon filtration of the enzy...
Guardado en:
| Autores principales: | , , |
|---|---|
| Publicado: |
1979
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v89_n3_p779_Galvagno http://hdl.handle.net/20.500.12110/paper_0006291X_v89_n3_p779_Galvagno |
| Aporte de: |
| Sumario: | Crude preparations of cyclic adenosine 3′, 5′-monophosphate phosphodiesterase were activated 1.5 to 2 fold by incubation with ATP, Mg2+ and cyclic AMP in a reaction which was both, time and temperature dependent. Cyclic AMP phosphodiesterase remained in an activated state upon filtration of the enzymatic preparation through Sephadex G-25 and ion-exchange chromatography. Activation of the enzyme in the presence of [γ 32P]ATP resulted in a significant amount of [32P] protein-bound radioactivity. Reversible deactivation of cyclic AMP phosphodiesterase was enhanced by Mg2+ and was accompanied by the release of [32P] protein bound radioactivity. The evidence is consistent with a mechanism for controlling cyclic AMP phosphodiesterase through phosphorylation-dephosphorylation sequence. © 1979. |
|---|