Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP

Cyclic AMP binding to Mucor rouxii protein kinase holoenzyme and free regulatory subunit was measured by the classical membrane filtration technique and by equilibrium dialysis. The results obtained demonstrate that the filtration method can be used without loss of any cyclic AMP binding site. Both...

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Detalles Bibliográficos
Autores principales: Moreno, Silvia, Pastori, Ricardo Luis
Publicado: 1983
Materias:
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v52_n1_p13_Moreno
http://hdl.handle.net/20.500.12110/paper_03008177_v52_n1_p13_Moreno
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spelling paper:paper_03008177_v52_n1_p13_Moreno2023-06-08T15:27:29Z Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP Moreno, Silvia Pastori, Ricardo Luis cyclic AMP histone protein kinase article binding site density gradient centrifugation dialysis enzymology filtration macromolecule metabolism methodology Mucor Binding Sites Centrifugation, Density Gradient Cyclic AMP Dialysis Filtration Histones Macromolecular Systems Mucor Protein Kinases Support, Non-U.S. Gov't Cyclic AMP binding to Mucor rouxii protein kinase holoenzyme and free regulatory subunit was measured by the classical membrane filtration technique and by equilibrium dialysis. The results obtained demonstrate that the filtration method can be used without loss of any cyclic AMP binding site. Both methods unambiguously demonstrate that the number of molecules of cyclic AMP bound to the holoenzyme are half of those bound to the regulatory subunit. This result suggests that unshielding of new cyclic AMP binding sites occurs upon dissociation of the ternary complex holoenzyme-cyclic AMP. © 1983 Martinus Nijhoff Publishers. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pastori, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1983 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v52_n1_p13_Moreno http://hdl.handle.net/20.500.12110/paper_03008177_v52_n1_p13_Moreno
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
histone
protein kinase
article
binding site
density gradient centrifugation
dialysis
enzymology
filtration
macromolecule
metabolism
methodology
Mucor
Binding Sites
Centrifugation, Density Gradient
Cyclic AMP
Dialysis
Filtration
Histones
Macromolecular Systems
Mucor
Protein Kinases
Support, Non-U.S. Gov't
spellingShingle cyclic AMP
histone
protein kinase
article
binding site
density gradient centrifugation
dialysis
enzymology
filtration
macromolecule
metabolism
methodology
Mucor
Binding Sites
Centrifugation, Density Gradient
Cyclic AMP
Dialysis
Filtration
Histones
Macromolecular Systems
Mucor
Protein Kinases
Support, Non-U.S. Gov't
Moreno, Silvia
Pastori, Ricardo Luis
Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
topic_facet cyclic AMP
histone
protein kinase
article
binding site
density gradient centrifugation
dialysis
enzymology
filtration
macromolecule
metabolism
methodology
Mucor
Binding Sites
Centrifugation, Density Gradient
Cyclic AMP
Dialysis
Filtration
Histones
Macromolecular Systems
Mucor
Protein Kinases
Support, Non-U.S. Gov't
description Cyclic AMP binding to Mucor rouxii protein kinase holoenzyme and free regulatory subunit was measured by the classical membrane filtration technique and by equilibrium dialysis. The results obtained demonstrate that the filtration method can be used without loss of any cyclic AMP binding site. Both methods unambiguously demonstrate that the number of molecules of cyclic AMP bound to the holoenzyme are half of those bound to the regulatory subunit. This result suggests that unshielding of new cyclic AMP binding sites occurs upon dissociation of the ternary complex holoenzyme-cyclic AMP. © 1983 Martinus Nijhoff Publishers.
author Moreno, Silvia
Pastori, Ricardo Luis
author_facet Moreno, Silvia
Pastori, Ricardo Luis
author_sort Moreno, Silvia
title Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
title_short Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
title_full Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
title_fullStr Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
title_full_unstemmed Protein kinase from Mucor rouxii - Unshielding of new cyclic AMP binding sites upon dissociation of the ternary complex holoenzyme-cyclic AMP
title_sort protein kinase from mucor rouxii - unshielding of new cyclic amp binding sites upon dissociation of the ternary complex holoenzyme-cyclic amp
publishDate 1983
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v52_n1_p13_Moreno
http://hdl.handle.net/20.500.12110/paper_03008177_v52_n1_p13_Moreno
work_keys_str_mv AT morenosilvia proteinkinasefrommucorrouxiiunshieldingofnewcyclicampbindingsitesupondissociationoftheternarycomplexholoenzymecyclicamp
AT pastoriricardoluis proteinkinasefrommucorrouxiiunshieldingofnewcyclicampbindingsitesupondissociationoftheternarycomplexholoenzymecyclicamp
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