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Abstract:

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.

Registro:

Documento: Artículo
Título:Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation
Autor:Galvagno, M.A.; Moreno, S.; Cantore, M.L.; Passeron, S.
Filiación:Departamento de Quimica Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 1428 Buenos Aires, Argentina
Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 1428 Buenos Aires, Argentina
Palabras clave: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
Año:1979
Volumen:89
Número:3
Página de inicio:779
Página de fin:785
DOI: http://dx.doi.org/10.1016/0006-291X(79)91846-1
Título revista:Biochemical and Biophysical Research Communications
Título revista abreviado:Biochem. Biophys. Res. Commun.
ISSN:0006291X
CODEN:BBRCA
CAS:3',5' cyclic nucleotide phosphodiesterase, 9040-59-9; magnesium, 7439-95-4; 3',5'-Cyclic-Nucleotide Phosphodiesterase, EC 3.1.4.17; Magnesium, 7439-95-4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v89_n3_p779_Galvagno

Referencias:

  • Nimmo, Cohen, (1977) Adv. Cycl. Nucl. Res, 8, pp. 145-166
  • Paveto, Epstein, Passeron, (1975) Arch. Biochem. Biophys, 169, pp. 449-457
  • Cantore, M. L., Galvagno, M. A. and Passeron, S. (1979) submitted for publication; Moreno, Paveto, Passeron, (1977) Arch. Biochem. Biophys, 180, pp. 225-231
  • Gnegy, Costa, Uzunov, (1976) Proc. Nat. Acad. Sci. U. S. A, 73, pp. 352-355
  • Chang, Marcus, Cuatrecasas, (1974) J. Biol. Chem, 249, pp. 6854-6865
  • Thompson, Appleman, (1971) Biochemistry, 10, pp. 311-316
  • Lowry, Rosebrough, Farr, Randall, (1951) J. Biol. Chem, 193, pp. 265-275

Citas:

---------- APA ----------
Galvagno, M.A., Moreno, S., Cantore, M.L. & Passeron, S. (1979) . Cyclic adenosine 3′, 5′-monophosphate phosphodiesterase from Mucor rouxii: Regulation of enzyme activity by phosphorylation and dephosphorylation. Biochemical and Biophysical Research Communications, 89(3), 779-785.
http://dx.doi.org/10.1016/0006-291X(79)91846-1
---------- CHICAGO ----------
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" . Biochemical and Biophysical Research Communications 89, no. 3 (1979) : 779-785.
http://dx.doi.org/10.1016/0006-291X(79)91846-1
---------- MLA ----------
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" . Biochemical and Biophysical Research Communications, vol. 89, no. 3, 1979, pp. 779-785.
http://dx.doi.org/10.1016/0006-291X(79)91846-1
---------- VANCOUVER ----------
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. Biochem. Biophys. Res. Commun. 1979;89(3):779-785.
http://dx.doi.org/10.1016/0006-291X(79)91846-1