Navegar

Colección

Datos Estadísticas

Artículo

El editor solo permite decargar el artículo en su versión post-print desde el repositorio. Por favor, si usted posee dicha versión, enviela a
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Partially purified cAMP phosphodiesterase from Mucor rouxii can be reversibly activated from 1.5- to 3-fold by treatment with MgATP, cAMP, and cAMP-dependent protein kinase, without change in its sedimentation behavior. Deactivation of activated enzyme can be observed in crude extracts under conditions which promote dephosphorylation; deactivation is prevented by 20 mm phosphate. cAMP phosphodiesterase can also be irreversibly activated by treatment with trypsin. The extent of activation by proteolysis is similar to that obtained by phosphorylation, but is accompanied by a decrease in the sedimentation coefficient of the enzyme. Activation by phosphorylation and proteolysis are not additive, suggesting that both mechanisms involve the same region of the enzyme molecule. © 1982.

Registro:

Documento: Artículo
Título:Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis
Autor:Moreno, S.; Galvagno, M.A.; Passeron, S.
Filiación:Programa de Regulación Hormonal y Metabólica, Departamento de Química Biológica y Departamento de Biología, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, 1428 Buenos Aires, Argentina
Palabras clave:adenosine triphosphate; cyclic amp; cyclic amp phosphodiesterase; protein kinase; fungus; nonhuman; 3',5'-Cyclic-Nucleotide Phosphodiesterase; Adenosine Triphosphate; Centrifugation, Density Gradient; Cyclic AMP; Enzyme Activation; Mucor; Phosphorylation; Protein Kinases; Support, Non-U.S. Gov't; Trypsin
Año:1982
Volumen:214
Número:2
Página de inicio:573
Página de fin:580
DOI: http://dx.doi.org/10.1016/0003-9861(82)90062-5
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; cyclic AMP phosphodiesterase, 9036-21-9; cyclic AMP, 60-92-4; protein kinase, 9026-43-1; 3',5'-Cyclic-Nucleotide Phosphodiesterase, EC 3.1.4.17; Adenosine Triphosphate, 56-65-5; Cyclic AMP, 60-92-4; Protein Kinases, EC 2.7.1.37; Trypsin, EC 3.4.21.4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v214_n2_p573_Moreno

Referencias:

  • Krebs, Beavo, Phosphorylation-Dephosphorylation of Enzymes (1979) Annual Review of Biochemistry, 48, pp. 23-59
  • Goldberg, St. John, Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2 (1976) Annual Review of Biochemistry, 45, pp. 748-803
  • Cantore, Galvagno, Passeron, (1980) Arch. Biochem. Biophys, 199, pp. 312-320
  • Galvagno, Moreno, Cantore, Passeron, (1979) Biochem. Biophys. Res. Commun, 89, pp. 779-785
  • Bartnicki-García, Nickerson, Induction of yeast-like development in Mucor by carbon dioxide. (1962) J Bacteriol, 84, pp. 829-840
  • Haidle, Stork, (1966) J. Bacteriol, 92, pp. 1236-1244
  • Moreno, Passeron, (1980) Arch. Biochem. Biophys, 199, pp. 321-330
  • Thompson, Appleman, (1971) Biochemistry, 10, pp. 311-316
  • Glynn, Chappell, (1964) Biochem. J, 90, pp. 147-149
  • Chang, Marcus, Cuatrecasas, (1974) J. Biol. Chem, 249, pp. 6854-6865
  • Bradford, (1976) Anal. Biochem, 72, pp. 248-254
  • Peterson, Sorber, (1962) Methods in Enzymology, 5, p. 6. , 2nd ed., P. Sydney, S.P. Colowick, N.O. Kaplan, Academic Press, New York
  • Cheung, (1969) Biochim. Biophys. Acta, 191, pp. 303-315
  • Sakai, Yamanaka, Tanaka, Makino, Kasai, (1977) Biochim. Biophys. Acta, 483, pp. 121-134
  • Moss, Manganiello, Vaughan, (1978) Biochim. Biophys. Acta, 541, pp. 279-287
  • Ball, Seth, Sanwal, (1980) J. Biol. Chem, 255, pp. 2962-2968
  • Loten, Francis, Corbin, (1980) J. Biol. Chem, 255, pp. 7838-7844
  • Marchmont, Houslay, (1980) Nature (London), 286, pp. 904-906
  • Bergstron, Ekman, Dahlkvist, Humble, Engstrom, Subtilisin-catalyzed removal of phosphorylated site of pig liver pyruvate kinase without inactivation of the enzyme (1975) FEBS Letters, 56, pp. 288-291
  • Fisher, Graves, Crittenden, Krebs, (1959) J. Biol. Chem, 234, pp. 1698-1704
  • Huston, Krebs, (1968) Biochemistry, 7, pp. 2116-2122
  • Huang, Cabib, (1974) J. Biol. Chem, 249, pp. 3858-3861
  • Nimmo, Cohen, (1974) FEBS Lett, 47, pp. 162-166
  • Abita, Milstein, Chang, Kaufman, (1976) J. Biol. Chem, 251, pp. 5310-5314

Citas:

---------- APA ----------
Moreno, S., Galvagno, M.A. & Passeron, S. (1982) . Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis. Archives of Biochemistry and Biophysics, 214(2), 573-580.
http://dx.doi.org/10.1016/0003-9861(82)90062-5
---------- CHICAGO ----------
Moreno, S., Galvagno, M.A., Passeron, S. "Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis" . Archives of Biochemistry and Biophysics 214, no. 2 (1982) : 573-580.
http://dx.doi.org/10.1016/0003-9861(82)90062-5
---------- MLA ----------
Moreno, S., Galvagno, M.A., Passeron, S. "Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis" . Archives of Biochemistry and Biophysics, vol. 214, no. 2, 1982, pp. 573-580.
http://dx.doi.org/10.1016/0003-9861(82)90062-5
---------- VANCOUVER ----------
Moreno, S., Galvagno, M.A., Passeron, S. Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis. Arch. Biochem. Biophys. 1982;214(2):573-580.
http://dx.doi.org/10.1016/0003-9861(82)90062-5