Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions

Autores
Chelala, C.A.; Torres, H.N.
Año de publicación
1970
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970.
Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
BBA - Enzymology 1970;198(3):504-513
Materia
adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00052744_v198_n3_p504_Chelala
Acceder
id BDUBAFCEN_54f3a54701c25d5a2bdf078d034c8b2c
oai_identifier_str paperaa:paper_00052744_v198_n3_p504_Chelala
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Regulation of skeletal muscle phosphorylase phosphatase activity. II. InterconversionsChelala, C.A.Torres, H.N.adenine nucleotideadenosine triphosphatecreatine phosphatecyclic AMPglucosyltransferaseguanine nucleotidemagnesiummercaptoethanolphosphatasephosphoruspyrimidine nucleotidepyrophosphateanimalarticleenzyme activationenzymologymusclepigeonAdenine NucleotidesAdenosine TriphosphateAnimalCyclic AMPCytosine NucleotidesDiphosphatesEnzyme ActivationGlucosyltransferasesGuanine NucleotidesMagnesiumMercaptoethanolMusclesPhosphocreatinePhosphoric Monoester HydrolasesPhosphorus IsotopesPigeonsUracil Nucleotides1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970.Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1970info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_ChelalaBBA - Enzymology 1970;198(3):504-513reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:09Zpaperaa:paper_00052744_v198_n3_p504_ChelalaInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:10.536Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
spellingShingle Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
Chelala, C.A.
adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
title_short Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_full Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_fullStr Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_full_unstemmed Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_sort Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
dc.creator.none.fl_str_mv Chelala, C.A.
Torres, H.N.
author Chelala, C.A.
author_facet Chelala, C.A.
Torres, H.N.
author_role author
author2 Torres, H.N.
author2_role author
dc.subject.none.fl_str_mv adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
topic adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
dc.description.none.fl_txt_mv 1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970.
Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970.
publishDate 1970
dc.date.none.fl_str_mv 1970
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala
url http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv BBA - Enzymology 1970;198(3):504-513
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
_version_ 1844618740331708416
score 13.070432

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