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The role of ATP and of a bound phosphoryl group acceptor on Ca binding and exchangeability in sarcoplasmic reticulum

Carvalho, A P ; Mota, A M

Archives of biochemistry and biophysics, January 1971, Vol.142(1), pp.201-12 [Periódico revisado por pares]

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  • Título:
    The role of ATP and of a bound phosphoryl group acceptor on Ca binding and exchangeability in sarcoplasmic reticulum
  • Autor: Carvalho, A P ; Mota, A M
  • Assuntos: Adenosine Triphosphate -- Metabolism ; Calcium -- Metabolism ; Endoplasmic Reticulum -- Metabolism ; Muscles -- Cytology ; Phosphoric Acids -- Metabolism
  • É parte de: Archives of biochemistry and biophysics, January 1971, Vol.142(1), pp.201-12
  • Descrição: Sarcoplasmic reticulum isolated from rabbit skeletal muscle has a bound phosphoryl group acceptor which is not removed by washing the membranes several times with 0.1 m KCl-5 m m imidazole, but it is destroyed by a commercial preparation of apyrase (1 mg of apyrase/5 mg of reticulum protein). Creatine phosphate (CP) plus creatine phosphokinase (CPK) support Ca uptake and cause all Ca bound to become exchangeable with 45Ca in the medium, but these effects are not observed if the acceptor is destroyed by apyrase. However, reticulum freed of phosphoryl group acceptor by treatment with apyrase can still take up Ca normally if ATP is present. Thus, the acceptor either is not fundamental for Ca uptake or it is replaced by ATP or its products of hydrolysis. The nonexchangeable bound Ca in reticulum preloaded with Ca and washed to remove free Ca 2+ and ATP is about 80% of the total Ca bound. This Ca is gradually lost over a period of 4 hr when the reticulum is placed in...
  • Idioma: Inglês

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