Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions

1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by inc...

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Autores principales: Chelala, C.A., Torres, H.N.
Formato: Artículo publishedVersion
Publicado: 1970
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v198_n3_p504_Chelala_oai
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spelling I28-R145-paper_00052744_v198_n3_p504_Chelala_oai2024-08-16 Chelala, C.A. Torres, H.N. 1970 1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970. Fil:Chelala, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar BBA - Enzymology 1970;198(3):504-513 adenine nucleotide adenosine triphosphate creatine phosphate cyclic AMP glucosyltransferase guanine nucleotide magnesium mercaptoethanol phosphatase phosphorus pyrimidine nucleotide pyrophosphate animal article enzyme activation enzymology muscle pigeon Adenine Nucleotides Adenosine Triphosphate Animal Cyclic AMP Cytosine Nucleotides Diphosphates Enzyme Activation Glucosyltransferases Guanine Nucleotides Magnesium Mercaptoethanol Muscles Phosphocreatine Phosphoric Monoester Hydrolases Phosphorus Isotopes Pigeons Uracil Nucleotides Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions 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_p504_Chelala_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
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
spellingShingle adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
Chelala, C.A.
Torres, H.N.
Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
topic_facet adenine nucleotide
adenosine triphosphate
creatine phosphate
cyclic AMP
glucosyltransferase
guanine nucleotide
magnesium
mercaptoethanol
phosphatase
phosphorus
pyrimidine nucleotide
pyrophosphate
animal
article
enzyme activation
enzymology
muscle
pigeon
Adenine Nucleotides
Adenosine Triphosphate
Animal
Cyclic AMP
Cytosine Nucleotides
Diphosphates
Enzyme Activation
Glucosyltransferases
Guanine Nucleotides
Magnesium
Mercaptoethanol
Muscles
Phosphocreatine
Phosphoric Monoester Hydrolases
Phosphorus Isotopes
Pigeons
Uracil Nucleotides
description 1. 1. The incubation of the pegion breast muscle homogenate at 37° resulted in a time-dependent decrease in phosphatase activity. This effect was stimulated by ATP, ADP, AMP, GTP, UTP, CTP or pyrophosphate. 2. 2. Reactivation of an inactive phosphorylase a phosphatase preparation was obtained by incubation with ATP-Mg2+. Phosphocreatine-Mg2+ or Mg2+ were also found to be effective in bringing about the reactivation of the enzyme. 3. 3. 3′,5′-Cyclic AMP decreased the yield of the active enzyme when it was added either at the beginning or during the activation reaction. © 1970.
format Artículo
Artículo
publishedVersion
author Chelala, C.A.
Torres, H.N.
author_facet Chelala, C.A.
Torres, H.N.
author_sort Chelala, C.A.
title Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_short Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_full Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_fullStr Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_full_unstemmed Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions
title_sort regulation of skeletal muscle phosphorylase phosphatase activity. ii. interconversions
publishDate 1970
url http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00052744_v198_n3_p504_Chelala_oai
work_keys_str_mv AT chelalaca regulationofskeletalmusclephosphorylasephosphataseactivityiiinterconversions
AT torreshn regulationofskeletalmusclephosphorylasephosphataseactivityiiinterconversions
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