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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann |
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todo:paper_08986568_v2_n4_p395_Guthmann2023-10-03T15:44:02Z Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii Guthmann, M. Pastori, R. Moreno, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M. Pastori, R. Moreno, S. 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. |
| format |
JOUR |
| author |
Guthmann, M. Pastori, R. Moreno, S. |
| author_facet |
Guthmann, M. Pastori, R. Moreno, S. |
| author_sort |
Guthmann, M. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_08986568_v2_n4_p395_Guthmann |
| work_keys_str_mv |
AT guthmannm polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii AT pastorir polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii AT morenos polyaminesandbasicproteinsstimulateactivationbycampandcatalyticactivitymucorrouxii |
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1807321675351457792 |