cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP
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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1981
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v101_n2_p663_Pastori http://hdl.handle.net/20.500.12110/paper_0006291X_v101_n2_p663_Pastori |
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paper:paper_0006291X_v101_n2_p663_Pastori2023-06-08T14:29:59Z cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP Pastori, Ricardo Luis Kerner, Néstor Alberto Moreno, Silvia cyclic AMP protein kinase article density gradient centrifugation enzymology isolation and purification macromolecule metabolism Mucor protein binding Centrifugation, Density Gradient Cyclic AMP Macromolecular Systems Mucor Protein Binding Protein Kinases Support, Non-U.S. Gov't 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. Fil:Pastori, R.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kerner, N. 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. 1981 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v101_n2_p663_Pastori http://hdl.handle.net/20.500.12110/paper_0006291X_v101_n2_p663_Pastori |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
cyclic AMP protein kinase article density gradient centrifugation enzymology isolation and purification macromolecule metabolism Mucor protein binding Centrifugation, Density Gradient Cyclic AMP Macromolecular Systems Mucor Protein Binding Protein Kinases Support, Non-U.S. Gov't |
| spellingShingle |
cyclic AMP protein kinase article density gradient centrifugation enzymology isolation and purification macromolecule metabolism Mucor protein binding Centrifugation, Density Gradient Cyclic AMP Macromolecular Systems Mucor Protein Binding Protein Kinases Support, Non-U.S. Gov't Pastori, Ricardo Luis Kerner, Néstor Alberto Moreno, Silvia cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| topic_facet |
cyclic AMP protein kinase article density gradient centrifugation enzymology isolation and purification macromolecule metabolism Mucor protein binding Centrifugation, Density Gradient Cyclic AMP Macromolecular Systems Mucor Protein Binding Protein Kinases Support, Non-U.S. Gov't |
| description |
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. |
| author |
Pastori, Ricardo Luis Kerner, Néstor Alberto Moreno, Silvia |
| author_facet |
Pastori, Ricardo Luis Kerner, Néstor Alberto Moreno, Silvia |
| author_sort |
Pastori, Ricardo Luis |
| title |
cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| title_short |
cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| title_full |
cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| title_fullStr |
cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| title_full_unstemmed |
cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP |
| title_sort |
camp-dependent protein kinase from mucor rouxii: physical evidence of a ternary complex holoenzyme-camp |
| publishDate |
1981 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v101_n2_p663_Pastori http://hdl.handle.net/20.500.12110/paper_0006291X_v101_n2_p663_Pastori |
| work_keys_str_mv |
AT pastoriricardoluis campdependentproteinkinasefrommucorrouxiiphysicalevidenceofaternarycomplexholoenzymecamp AT kernernestoralberto campdependentproteinkinasefrommucorrouxiiphysicalevidenceofaternarycomplexholoenzymecamp AT morenosilvia campdependentproteinkinasefrommucorrouxiiphysicalevidenceofaternarycomplexholoenzymecamp |
| _version_ |
1768544391723483136 |