Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein

Protein kinase and cyclic adenosine 3′,5′-monophosphate (cAMP) binding activities have been detected in cell extracts of the dimorphic fungus Mucor rouxii. The subcellular distribution of both activities indicates that most of the binding protein is in the high-speed supernatant (S100), while about...

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Autores principales: Moreno, S., Paveto, C., Passeron, S.
Formato: JOUR
Materias:
cyclic amp
protein kinase
in vitro study
microorganism
mucor rouxii
theoretical study
Cyclic AMP
Kinetics
Mucor
Protein Binding
Protein Kinases
Receptors, Cyclic AMP
Subcellular Fractions
Theophylline
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v180_n2_p225_Moreno
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00039861_v180_n2_p225_Moreno
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spelling todo:paper_00039861_v180_n2_p225_Moreno2023-10-03T13:56:52Z Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein Moreno, S. Paveto, C. Passeron, S. cyclic amp protein kinase in vitro study microorganism mucor rouxii theoretical study Cyclic AMP Kinetics Mucor Protein Binding Protein Kinases Receptors, Cyclic AMP Subcellular Fractions Theophylline Protein kinase and cyclic adenosine 3′,5′-monophosphate (cAMP) binding activities have been detected in cell extracts of the dimorphic fungus Mucor rouxii. The subcellular distribution of both activities indicates that most of the binding protein is in the high-speed supernatant (S100), while about 70% of the total protein kinase activity remains in particulate fractions. S100 preparations have been analyzed by diethylaminoethyl cellulose column chromatography. Binding activity can be resolved in two peaks (A and B) and protein kinase in three peaks (I, II, and III). Peaks I and II are casein dependent and insensitive to cAMP. Peak III utilizes histone as substrate and is activated (two- to fourfold) by cAMP. Theophylline strongly inhibits cAMP binding activity and mimics the effect of cAMP on cAMP-dependent protein kinase. The possible relationship between cAMP binding activity and cAMP-dependent protein kinase is suggested. © 1977. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Paveto, C. 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_00039861_v180_n2_p225_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
protein kinase
in vitro study
microorganism
mucor rouxii
theoretical study
Cyclic AMP
Kinetics
Mucor
Protein Binding
Protein Kinases
Receptors, Cyclic AMP
Subcellular Fractions
Theophylline
spellingShingle cyclic amp
protein kinase
in vitro study
microorganism
mucor rouxii
theoretical study
Cyclic AMP
Kinetics
Mucor
Protein Binding
Protein Kinases
Receptors, Cyclic AMP
Subcellular Fractions
Theophylline
Moreno, S.
Paveto, C.
Passeron, S.
Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
topic_facet cyclic amp
protein kinase
in vitro study
microorganism
mucor rouxii
theoretical study
Cyclic AMP
Kinetics
Mucor
Protein Binding
Protein Kinases
Receptors, Cyclic AMP
Subcellular Fractions
Theophylline
description Protein kinase and cyclic adenosine 3′,5′-monophosphate (cAMP) binding activities have been detected in cell extracts of the dimorphic fungus Mucor rouxii. The subcellular distribution of both activities indicates that most of the binding protein is in the high-speed supernatant (S100), while about 70% of the total protein kinase activity remains in particulate fractions. S100 preparations have been analyzed by diethylaminoethyl cellulose column chromatography. Binding activity can be resolved in two peaks (A and B) and protein kinase in three peaks (I, II, and III). Peaks I and II are casein dependent and insensitive to cAMP. Peak III utilizes histone as substrate and is activated (two- to fourfold) by cAMP. Theophylline strongly inhibits cAMP binding activity and mimics the effect of cAMP on cAMP-dependent protein kinase. The possible relationship between cAMP binding activity and cAMP-dependent protein kinase is suggested. © 1977.
format JOUR
author Moreno, S.
Paveto, C.
Passeron, S.
author_facet Moreno, S.
Paveto, C.
Passeron, S.
author_sort Moreno, S.
title Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
title_short Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
title_full Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
title_fullStr Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
title_full_unstemmed Multiple protein kinase activities in the dimorphic fungus Mucor rouxii. Comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
title_sort multiple protein kinase activities in the dimorphic fungus mucor rouxii. comparison with a cyclic adenosine 3′,5′-monophosphate binding protein
url http://hdl.handle.net/20.500.12110/paper_00039861_v180_n2_p225_Moreno
work_keys_str_mv AT morenos multipleproteinkinaseactivitiesinthedimorphicfungusmucorrouxiicomparisonwithacyclicadenosine35monophosphatebindingprotein
AT pavetoc multipleproteinkinaseactivitiesinthedimorphicfungusmucorrouxiicomparisonwithacyclicadenosine35monophosphatebindingprotein
AT passerons multipleproteinkinaseactivitiesinthedimorphicfungusmucorrouxiicomparisonwithacyclicadenosine35monophosphatebindingprotein
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