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...
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todo:paper_0006291X_v89_n3_p779_Galvagno2023-10-03T14:04:11Z Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation Galvagno, M.A. Moreno, S. Cantore, M.L. Passeron, S. 3',5' cyclic nucleotide phosphodiesterase magnesium article enzyme activation enzymology isolation and purification kinetics metabolism Mucor phosphorylation 3',5'-Cyclic-Nucleotide Phosphodiesterase Enzyme Activation Kinetics Magnesium Mucor Phosphorylation 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. Fil:Galvagno, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cantore, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v89_n3_p779_Galvagno |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
3',5' cyclic nucleotide phosphodiesterase magnesium article enzyme activation enzymology isolation and purification kinetics metabolism Mucor phosphorylation 3',5'-Cyclic-Nucleotide Phosphodiesterase Enzyme Activation Kinetics Magnesium Mucor Phosphorylation |
| spellingShingle |
3',5' cyclic nucleotide phosphodiesterase magnesium article enzyme activation enzymology isolation and purification kinetics metabolism Mucor phosphorylation 3',5'-Cyclic-Nucleotide Phosphodiesterase Enzyme Activation Kinetics Magnesium Mucor Phosphorylation Galvagno, M.A. Moreno, S. Cantore, M.L. Passeron, S. Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| topic_facet |
3',5' cyclic nucleotide phosphodiesterase magnesium article enzyme activation enzymology isolation and purification kinetics metabolism Mucor phosphorylation 3',5'-Cyclic-Nucleotide Phosphodiesterase Enzyme Activation Kinetics Magnesium Mucor Phosphorylation |
| description |
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. |
| format |
JOUR |
| author |
Galvagno, M.A. Moreno, S. Cantore, M.L. Passeron, S. |
| author_facet |
Galvagno, M.A. Moreno, S. Cantore, M.L. Passeron, S. |
| author_sort |
Galvagno, M.A. |
| title |
Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| title_short |
Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| title_full |
Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| title_fullStr |
Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| title_full_unstemmed |
Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation |
| title_sort |
cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from mucor rouxii: regulation of enzyme activity by phosphorylation and dephosphorylation |
| url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v89_n3_p779_Galvagno |
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