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Abstract:

Yeast cells of the dimorphic fungus Mucor rouxii have been permeabilized by treatment with toluene:ethanol. The permeabilization allowed the in situ measurement of pyruvate kinase, cAMP phosphodiesterase and adenylate cyclase activities. Using a small peptide as substrate, cAMP dependent protein kinase activity could also be measured. Permeabilized cells showed higher cAMP phosphodiesterase and adenylate cyclase activities than cellular homogenates. The main catalytic properties of the enzymes were similar to that previously found in in vitro studies. © 1982.

Registro:

Documento: Artículo
Título:In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii
Autor:Maggese, M.C.; Galvagno, M.A.; Cantore, M.L.; Passeron, S.
Filiación:Programa de Regulación Hormonal y Metabólica, Departamento de Química Biológica y Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, 1428 Buenos Aires, Argentina
Career Investigator of the Consejo Nacional de Investigaciones Científicas y Técnicas, Argentina
Palabras clave:3',5' cyclic nucleotide phosphodiesterase; adenylate cyclase; cyclic AMP; protein kinase; pyruvate kinase; toluene; article; comparative study; metabolism; Mucor; permeability; 3',5'-Cyclic-Nucleotide Phosphodiesterase; Adenylate Cyclase; Comparative Study; Cyclic AMP; Mucor; Permeability; Protein Kinases; Pyruvate Kinase; Support, Non-U.S. Gov't; Toluene
Año:1982
Volumen:6
Número:12
Página de inicio:1101
Página de fin:1108
DOI: http://dx.doi.org/10.1016/0309-1651(82)90027-3
Título revista:Cell Biology International Reports
Título revista abreviado:Cell Biol. Int. Rep.
ISSN:03091651
CODEN:CBRPD
CAS:3',5' cyclic nucleotide phosphodiesterase, 9040-59-9; adenylate cyclase, 9012-42-4; cyclic AMP, 60-92-4; protein kinase, 9026-43-1; pyruvate kinase, 9001-59-6; toluene, 108-88-3; 3',5'-Cyclic-Nucleotide Phosphodiesterase, EC 3.1.4.17; Adenylate Cyclase, EC 4.6.1.1; Cyclic AMP, 60-92-4; Protein Kinases, EC 2.7.1.37; Pyruvate Kinase, EC 2.7.1.40; Toluene, 108-88-3
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03091651_v6_n12_p1101_Maggese

Referencias:

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  • Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Analytical Biochemistry, 72, pp. 248-254
  • Cantore, Galvagno, Passeron, Variations in the levels of cyclic adenosine 3′–5′ monophosphate and in the activities of adenylate cyclase and cyclic adenosine 3′–5′ monophosphate phosphodiesterase during aerobic morphogenesis of Mucor rouxii (1980) Archives of Biochemistry and Biophysics, 199, pp. 312-320
  • Cantore, Passeron, Kinetic properties solubilization and molecular characterization of Mucor rouxii adenylate cyclase (1982) Arch Biochem Biophys, , in press
  • Felix, Permeabilized cells (1982) Analytical Biochemistry, 120, pp. 211-234
  • Galvagno, Moreno, Cantore, Passeron, Cyclic adenosine 3′–5′ monophosphate phosphodiesterase from Mucor rouxii: regulation of enzyme activity by phosphorylation and dephosphorylation (1979) Biochemical and Biophysical Research Communications, 89, pp. 779-785
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  • Kemp, Clark, Adrenergic control of the cyclic AMP-dependent protein kinase and pyruvate kinase in isolated hepatocytes (1978) Journal of Biological Chemistry, 253, pp. 5147-5154
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  • Moreno, Passeron, Further studies on cyclic adenosine 3′–5′ monophosphate protein kinase from the dimorphic fungus Mucor rouxii (1980) Archives of Biochemistry and Biophysics, 199, pp. 321-330
  • Moreno, Paveto, Passeron, Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′–5′-monophosphate binding protein (1977) Archives of Biochemistry and Biophysics, 180, pp. 225-231
  • Pastori, Kerner, Moreno, Passeron, cAMP-dependent protein kinase from Mucor rouxii: physical evidence of a ternary complex holoenzyme-cAMP (1981) Biochemical and Biophysical Research Communications, 101, pp. 663-671
  • Paveto, Epstein, Passeron, Studies on cyclic adenosine 3′,5′-monophosphate levels, adenylate cyclase and phosphodiesterase activities in the dimorphic fungus Mucor rouxii (1975) Archives of Biochemistry and Biophysics, 169, pp. 449-456
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Citas:

---------- APA ----------
Maggese, M.C., Galvagno, M.A., Cantore, M.L. & Passeron, S. (1982) . In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii. Cell Biology International Reports, 6(12), 1101-1108.
http://dx.doi.org/10.1016/0309-1651(82)90027-3
---------- CHICAGO ----------
Maggese, M.C., Galvagno, M.A., Cantore, M.L., Passeron, S. "In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii" . Cell Biology International Reports 6, no. 12 (1982) : 1101-1108.
http://dx.doi.org/10.1016/0309-1651(82)90027-3
---------- MLA ----------
Maggese, M.C., Galvagno, M.A., Cantore, M.L., Passeron, S. "In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii" . Cell Biology International Reports, vol. 6, no. 12, 1982, pp. 1101-1108.
http://dx.doi.org/10.1016/0309-1651(82)90027-3
---------- VANCOUVER ----------
Maggese, M.C., Galvagno, M.A., Cantore, M.L., Passeron, S. In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii. Cell Biol. Int. Rep. 1982;6(12):1101-1108.
http://dx.doi.org/10.1016/0309-1651(82)90027-3