Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP puls protamine or histone. full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation...

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Autores principales: Guthmann, Marcelo, Pastori, Ricardo Luis, Moreno, Silvia
Publicado: 1990
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v2_n4_p395_Guthmann
http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann
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spelling paper:paper_08986568_v2_n4_p395_Guthmann2023-06-08T15:49:27Z Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii Guthmann, Marcelo Pastori, Ricardo Luis Moreno, Silvia cAMP-dependent Mucor rouxii polyamines polycations Protein kinase cyclic amp polyamine protein kinase animal cell article enzyme activation fungus nonhuman priority journal Animal Cattle Cyclic AMP Enzyme Activation In Vitro Kinetics Mucor Myocardium Polyamines Protein Kinases Proteins Substrate Specificity Support, Non-U.S. Gov't Amylomyces rouxii Animalia Bovinae Fungi Mucor Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP puls protamine or histone. full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-riche histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3 fold the Vmax of kemptide phosphorylation by the ree catalytic subunits of both Mucor and bovine heart protein kinase; 10 μM polyarginine inhibited completely and activity of both enyzmes. © 1990. Fil:Guthmann, M. 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. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v2_n4_p395_Guthmann http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic cAMP-dependent
Mucor rouxii
polyamines
polycations
Protein kinase
cyclic amp
polyamine
protein kinase
animal cell
article
enzyme activation
fungus
nonhuman
priority journal
Animal
Cattle
Cyclic AMP
Enzyme Activation
In Vitro
Kinetics
Mucor
Myocardium
Polyamines
Protein Kinases
Proteins
Substrate Specificity
Support, Non-U.S. Gov't
Amylomyces rouxii
Animalia
Bovinae
Fungi
Mucor
spellingShingle cAMP-dependent
Mucor rouxii
polyamines
polycations
Protein kinase
cyclic amp
polyamine
protein kinase
animal cell
article
enzyme activation
fungus
nonhuman
priority journal
Animal
Cattle
Cyclic AMP
Enzyme Activation
In Vitro
Kinetics
Mucor
Myocardium
Polyamines
Protein Kinases
Proteins
Substrate Specificity
Support, Non-U.S. Gov't
Amylomyces rouxii
Animalia
Bovinae
Fungi
Mucor
Guthmann, Marcelo
Pastori, Ricardo Luis
Moreno, Silvia
Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
topic_facet cAMP-dependent
Mucor rouxii
polyamines
polycations
Protein kinase
cyclic amp
polyamine
protein kinase
animal cell
article
enzyme activation
fungus
nonhuman
priority journal
Animal
Cattle
Cyclic AMP
Enzyme Activation
In Vitro
Kinetics
Mucor
Myocardium
Polyamines
Protein Kinases
Proteins
Substrate Specificity
Support, Non-U.S. Gov't
Amylomyces rouxii
Animalia
Bovinae
Fungi
Mucor
description Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP puls protamine or histone. full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-riche histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3 fold the Vmax of kemptide phosphorylation by the ree catalytic subunits of both Mucor and bovine heart protein kinase; 10 μM polyarginine inhibited completely and activity of both enyzmes. © 1990.
author Guthmann, Marcelo
Pastori, Ricardo Luis
Moreno, Silvia
author_facet Guthmann, Marcelo
Pastori, Ricardo Luis
Moreno, Silvia
author_sort Guthmann, Marcelo
title Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
title_short Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
title_full Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
title_fullStr Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
title_full_unstemmed Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii
title_sort polyamines and basic proteins stimulate activation by camp and catalytic activity mucor rouxii
publishDate 1990
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v2_n4_p395_Guthmann
http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann
work_keys_str_mv AT guthmannmarcelo polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii
AT pastoriricardoluis polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii
AT morenosilvia polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii
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