cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP

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Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with...

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Detalles Bibliográficos
Autor principal: Pastori, R.L
Otros Autores: Kerner, N., Moreno, S., Passeron, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1981
Acceso en línea:Registro en Scopus
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Aporte de:Registro referencial: Solicitar el recurso aquí
Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-0019891331 
024 7 |2 cas  |a cyclic AMP, 60-92-4; protein kinase, 9026-43-1; Cyclic AMP, 60-92-4; Macromolecular Systems; Protein Kinases, EC 2.7.1.37 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BBRCA 
100 1 |a Pastori, R.L. 
245 1 0 |a cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP 
260 |c 1981 
270 1 0 |m Pastori, R.L.; Programa de Regulación Hormonal y Metabólica, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Krebs, Beavo, (1979) Annu. Rev. Biochem, 48, pp. 923-959 
504 |a Builder, Beavo, Krebs, (1980) J. Biol. Chem, 255, pp. 2350-2354 
504 |a Corbin, Sugden, West, Flockhart, Lincoln, Mc. Carthy, (1978) J. Biol. Chem, 253, pp. 3997-4003 
504 |a Builder, Beavo, Krebs, (1980) J. Biol. Chem, 255, pp. 3514-3519 
504 |a Ogez, Segel, (1976) J. Biol. Chem, 251, pp. 4551-4556 
504 |a Boeynaems, Dumont, (1977) Mol. Cell. Endocrinol, 7, pp. 275-295 
504 |a Tsuzuki, Kiger, Jr., (1978) Biochemistry, 17, pp. 2961-2970 
504 |a Chau, Huang, Romero, Biltonen, Huang, (1980) Biochemistry, 19, pp. 924-928 
504 |a Granot, Mildvan, Kaiser, (1980) Arch. Biochem. Biophys, 205, pp. 1-17 
504 |a Armstrong, Kaiser, (1978) Biochemistry, 17, pp. 2840-2845 
504 |a Huang, Froehlich, Charlton, Huang, (1977) Fed. Proc, 36, p. 690 
504 |a Moreno, Paveto, Passeron, (1976) Acta Physiol. Latin, 26, pp. 343-348 
504 |a Moreno, Passeron, (1980) Arch. Biochem. Biophys, 199, pp. 321-330 
504 |a Galvagno, Moreno, Cantore, Passeron, (1979) Biochem. Biophys. Res. Commun, 89, pp. 779-785 
504 |a Chang, Marcus, Cuatrecasas, (1974) J. Biol. Chem, 249, pp. 6854-6865 
504 |a Glass, Masarachia, Ferramisco, Kemp, (1978) Anal. Biochem, 87, pp. 566-575 
504 |a Gilman, (1970) Proc. Natl. Acad. Sci. U.S.A, 67, pp. 305-312 
504 |a Davis, (1964) Ann. N. Y. Acad. Sci, 121, pp. 404-427 
504 |a Bradford, (1976) Anal. Biochem, 72, pp. 248-254 
504 |a Sudgen, Corbin, (1976) Biochem. J, 159, pp. 423-437 
504 |a Døskeland, Ueland, Haga, Factors affecting the binding of [3H]adenosine 3':5'-cyclic monophosphate to protein kinase from bovine adrenal cortex. (1977) Biochem J, 161, pp. 653-665 
504 |a Øgreid, Døskeland, (1980) FEBS Lett, 121, pp. 340-344 
504 |a Potter, Stafford, Taylor, (1978) Arch. Biochem. Biophys, 190, pp. 174-180 
504 |a Rannels, Corbin, (1979) J. Biol. Chem, 254, pp. 8605-8610 
504 |a Potter, R.L. and Taylor, S. (1980) 255, 9706-9712; Gagelmann, Reed, Kubler, Pyerin, Kinzel, (1980) Proc. Natl. Acad. Sci. U.S.A, 77, pp. 2492-2496 
520 3 |a Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates the holoenzyme into free regulatory (R) and catalytic (C) subunits. At 4°C, cAMP bound to the holoenzyme is readily exchangeable with unlabeled cAMP (half life 2.5 min), while the nucleotide bound to the R subunit has a very slow exchange rate (half life 210 min). The amount of cAMP bound to R subunit is approximately twice the amount bound to holoenzyme at saturation. © 1981.  |l eng 
536 |a Detalles de la financiación: Secretaria de Estado de Ciência e Tecnologia, SECT 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgements: This work has been supported by grants from the Consejo National de Investigaciones Cientificas y Tecnicas, (CONICET), Secretaria de Estado de Ciencia y Tecnologia and ComisiBn National de Energia AtBmica. N.K. is a post-graduate Fellow and S.P. and S.M. are Career Investigators of CONICET. The authors wish to express their gratitude to Dr. C.E. Cardini his constant and enthusiastic support. 
593 |a Programa de Regulación Hormonal y Metabólica, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina 
690 1 0 |a CYCLIC AMP 
690 1 0 |a PROTEIN KINASE 
690 1 0 |a ARTICLE 
690 1 0 |a DENSITY GRADIENT CENTRIFUGATION 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a ISOLATION AND PURIFICATION 
690 1 0 |a MACROMOLECULE 
690 1 0 |a METABOLISM 
690 1 0 |a MUCOR 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a CENTRIFUGATION, DENSITY GRADIENT 
690 1 0 |a CYCLIC AMP 
690 1 0 |a MACROMOLECULAR SYSTEMS 
690 1 0 |a MUCOR 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN KINASES 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
700 1 |a Kerner, N. 
700 1 |a Moreno, S. 
700 1 |a Passeron, S. 
773 0 |d 1981  |g v. 101  |h pp. 663-671  |k n. 2  |p Biochem. Biophys. Res. Commun.  |x 0006291X  |w (AR-BaUEN)CENRE-905  |t Biochemical and Biophysical Research Communications 
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856 4 0 |u https://doi.org/10.1016/0006-291X(81)91310-3  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_0006291X_v101_n2_p663_Pastori  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v101_n2_p663_Pastori  |y Registro en la Biblioteca Digital 
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963 |a VARI 
999 |c 62242 

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