Regulation of skeletal muscle phosphorylase phosphatase activity. II. Interconversions

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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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Detalles Bibliográficos
Autores principales: Chelala, C.A., Torres, H.N.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00052744_v198_n3_p504_Chelala
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

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