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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00052744_v198_n3_p495_Torres
Ver los metadatos del registro completo
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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/ar2025-09-29T13:43:09Zpaperaa: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:18962025-09-29 13:43:10.611Biblioteca 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 |
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1844618740371554305 |
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13.070432 |