Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms

Autores
Torres, H.N.; Chelala, C.A.
Año de publicación
1970
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. The inactivation of phosphorylase a phosphatase decreased the maximum velocity of the phosphorylase a to phosphorylase b conversion reaction when it was assayed at different phosphorylase a concectrations. 2. 2. Maximal phosphorylase a phosphatase activities were found between pH 8 and 8.3. Inactivation of the phosphorylase a phosphatase led to a decrease in the activity in all the pH ranges tested. 3. 3. Theophylline and caffeine stimulated the phosphorylase a phosphatase. The effect of these substances was exerted in the reaction assay of the enzyme. 4. 4. ATP, ADP, AMP, GTP, UTP, CTP and pyrophosphate were found to decrease the rate of the reaction catalyzed by phosphorylase a phosphatase. This effect showed a striking parallelism with the capacity of these compounds to stimulate the phosphatase inactivation. © 1970.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
BBA - Enzymology 1970;198(3):495-503
Materia
adenine nucleotide
caffeine
glucosyltransferase
guanine nucleotide
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
theophylline
animal
article
chemistry
enzyme activation
enzymology
kinetics
muscle
pH
rabbit
Adenine Nucleotides
Animal
Caffeine
Chemistry
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Hydrogen-Ion Concentration
Kinetics
Muscles
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Rabbits
Theophylline
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_p495_Torres
Acceder
id BDUBAFCEN_2ec347de6fa4713a28ab1ee6eccac15c
oai_identifier_str paperaa:paper_00052744_v198_n3_p495_Torres
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive formsTorres, H.N.Chelala, C.A.adenine nucleotidecaffeineglucosyltransferaseguanine nucleotidephosphatasephosphoruspyrimidine nucleotidepyrophosphatetheophyllineanimalarticlechemistryenzyme activationenzymologykineticsmusclepHrabbitAdenine NucleotidesAnimalCaffeineChemistryCytosine NucleotidesDiphosphatesEnzyme ActivationGlucosyltransferasesGuanine NucleotidesHydrogen-Ion ConcentrationKineticsMusclesPhosphoric Monoester HydrolasesPhosphorus IsotopesRabbitsTheophyllineUracil Nucleotides1. 1. The inactivation of phosphorylase a phosphatase decreased the maximum velocity of the phosphorylase a to phosphorylase b conversion reaction when it was assayed at different phosphorylase a concectrations. 2. 2. Maximal phosphorylase a phosphatase activities were found between pH 8 and 8.3. Inactivation of the phosphorylase a phosphatase led to a decrease in the activity in all the pH ranges tested. 3. 3. Theophylline and caffeine stimulated the phosphorylase a phosphatase. The effect of these substances was exerted in the reaction assay of the enzyme. 4. 4. ATP, ADP, AMP, GTP, UTP, CTP and pyrophosphate were found to decrease the rate of the reaction catalyzed by phosphorylase a phosphatase. This effect showed a striking parallelism with the capacity of these compounds to stimulate the phosphatase inactivation. © 1970.Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Chelala, C.A. 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_p495_TorresBBA - Enzymology 1970;198(3):495-503reponame: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/ar2025-10-23T11:18:34Zpaperaa:paper_00052744_v198_n3_p495_TorresInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:36.162Biblioteca 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. I. Kinetic properties of the active and inactive forms
title Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
spellingShingle Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
Torres, H.N.
adenine nucleotide
caffeine
glucosyltransferase
guanine nucleotide
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
theophylline
animal
article
chemistry
enzyme activation
enzymology
kinetics
muscle
pH
rabbit
Adenine Nucleotides
Animal
Caffeine
Chemistry
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Hydrogen-Ion Concentration
Kinetics
Muscles
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Rabbits
Theophylline
Uracil Nucleotides
title_short Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
title_full Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
title_fullStr Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
title_full_unstemmed Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
title_sort Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
dc.creator.none.fl_str_mv Torres, H.N.
Chelala, C.A.
author Torres, H.N.
author_facet Torres, H.N.
Chelala, C.A.
author_role author
author2 Chelala, C.A.
author2_role author
dc.subject.none.fl_str_mv adenine nucleotide
caffeine
glucosyltransferase
guanine nucleotide
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
theophylline
animal
article
chemistry
enzyme activation
enzymology
kinetics
muscle
pH
rabbit
Adenine Nucleotides
Animal
Caffeine
Chemistry
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Hydrogen-Ion Concentration
Kinetics
Muscles
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Rabbits
Theophylline
Uracil Nucleotides
topic adenine nucleotide
caffeine
glucosyltransferase
guanine nucleotide
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
theophylline
animal
article
chemistry
enzyme activation
enzymology
kinetics
muscle
pH
rabbit
Adenine Nucleotides
Animal
Caffeine
Chemistry
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Hydrogen-Ion Concentration
Kinetics
Muscles
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Rabbits
Theophylline
Uracil Nucleotides
dc.description.none.fl_txt_mv 1. 1. The inactivation of phosphorylase a phosphatase decreased the maximum velocity of the phosphorylase a to phosphorylase b conversion reaction when it was assayed at different phosphorylase a concectrations. 2. 2. Maximal phosphorylase a phosphatase activities were found between pH 8 and 8.3. Inactivation of the phosphorylase a phosphatase led to a decrease in the activity in all the pH ranges tested. 3. 3. Theophylline and caffeine stimulated the phosphorylase a phosphatase. The effect of these substances was exerted in the reaction assay of the enzyme. 4. 4. ATP, ADP, AMP, GTP, UTP, CTP and pyrophosphate were found to decrease the rate of the reaction catalyzed by phosphorylase a phosphatase. This effect showed a striking parallelism with the capacity of these compounds to stimulate the phosphatase inactivation. © 1970.
Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. The inactivation of phosphorylase a phosphatase decreased the maximum velocity of the phosphorylase a to phosphorylase b conversion reaction when it was assayed at different phosphorylase a concectrations. 2. 2. Maximal phosphorylase a phosphatase activities were found between pH 8 and 8.3. Inactivation of the phosphorylase a phosphatase led to a decrease in the activity in all the pH ranges tested. 3. 3. Theophylline and caffeine stimulated the phosphorylase a phosphatase. The effect of these substances was exerted in the reaction assay of the enzyme. 4. 4. ATP, ADP, AMP, GTP, UTP, CTP and pyrophosphate were found to decrease the rate of the reaction catalyzed by phosphorylase a phosphatase. This effect showed a striking parallelism with the capacity of these compounds to stimulate the phosphatase inactivation. © 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_p495_Torres
url http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
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):495-503
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_ 1846784882342100993
score 12.982451

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