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

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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. In...

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Autores principales: Torres, H.N., Chelala, C.A.
Formato: Artículo publishedVersion
Publicado: 1970
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v198_n3_p495_Torres_oai
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Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
id I28-R145-paper_00052744_v198_n3_p495_Torres_oai
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spelling I28-R145-paper_00052744_v198_n3_p495_Torres_oai2024-08-16 Torres, H.N. Chelala, C.A. 1970 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. application/pdf http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar BBA - Enzymology 1970;198(3):495-503 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 Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v198_n3_p495_Torres_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
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
spellingShingle 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
Torres, H.N.
Chelala, C.A.
Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
topic_facet 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
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.
format Artículo
Artículo
publishedVersion
author Torres, H.N.
Chelala, C.A.
author_facet Torres, H.N.
Chelala, C.A.
author_sort Torres, H.N.
title Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
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
publishDate 1970
url http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v198_n3_p495_Torres_oai
work_keys_str_mv AT torreshn regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms
AT chelalaca regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms
_version_ 1809356953096290304

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