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: | , |
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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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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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