Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms
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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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n3_p495_Torres http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres |
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paper:paper_00052744_v198_n3_p495_Torres2023-06-08T14:29:54Z Regulation of skeletal muscle phosphorylase phosphatase activity. I. Kinetic properties of the active and inactive forms Torres, Héctor Norberto Chelala, César 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. 1970 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n3_p495_Torres 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, Héctor Norberto Chelala, César 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. |
author |
Torres, Héctor Norberto Chelala, César A. |
author_facet |
Torres, Héctor Norberto Chelala, César A. |
author_sort |
Torres, Héctor Norberto |
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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v198_n3_p495_Torres http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p495_Torres |
work_keys_str_mv |
AT torreshectornorberto regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms AT chelalacesara regulationofskeletalmusclephosphorylasephosphataseactivityikineticpropertiesoftheactiveandinactiveforms |
_version_ |
1768542625142407168 |