Effect of Calcium-Binding Protein on the Activation of Phosphorylase a in Rat Hepatic Participate Glycogen by Ca^<2+>(Biological)

  • 山口 正義
    Department of Environmental Biochemistry and Toxicology, Shizuoka College of Pharmacy
  • 柴野 広介
    Department of Environmental Biochemistry and Toxicology, Shizuoka College of Pharmacy

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The effect of a calcium-binding protein(CaBP) isolated from rat liver cytosol on phos- phorylase a activity in the hepatic participate glycogen was investigated. The particulate glycogen phosphorylase a activity was significantly increased by addition of Ca^<2+> in the range of 1.0-10^3μM. This increase was not prevented by the presence of N-(6-arninohexyl)-5-chloro-l- napthalenesulfonamide(W-7 100μM), an inhibitor of calmodulin. The elevation of phosphorylase a activity by 10 μM Ca^<2+> addition was significantly inhibited by the presence of CaBP at a concentration of greater than 3.0 μM. This inhibition was complete at 7.0μM CaBP. CaBP itself had no effect on the enzyme activity. Of various metals (20 μM) .used, addition of Zn^<2+> caused a significant decrease of the particulate glycogen phosphorylase a activity, while Mg^<2+>, Mn^<2+> and Cd^<2+> had no effect on the enzyme activity. The presence of 3.5μM CaBP did not block the inhibition of the enzyme activity by Zn^<2+> addition, indicating that CaBP uniquely reverses the Ca^<2+> effect. The present study suggests that CaBP regulates the effect of Ca^<2+> on phosphorylase a activity in the hepatic particulate glycogen of rats.

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