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:	JOUR
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
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00052744_v198_n3_p495_Torres
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spelling	todo:paper_00052744_v198_n3_p495_Torres2023-10-03T14:03:23Z Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms Torres, H.N. Chelala, C.A. 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (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	JOUR
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
url	http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres
work_keys_str_mv	AT torreshn regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms AT chelalaca regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms
_version_	1807316188111306752

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

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