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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide.

Addition of glucagon to isolated hepatocytes increased glycogenolysis and phosphorylase a in a proportional manner. KCN caused slightly more glycogenolysis at considerably lower levels of phosphorylase a; the discrepancy was most pronounced after pretreatment of the hepatocytes with EGTA. When incubated with tagatose, the hepatocytes accumulated tagatose 1-phosphate, a presumed inhibitor of phosphorylase a. In these conditions the glucagon-induced glycogenolysis was blocked, but the glycogen loss caused by KCN or anoxia was not affected. Cyanide and anoxia may allow phosphorylase b and a to become equally active, or they may trigger a non-phosphorolytic glycogenolysis.[1]

References

  1. On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide. Bollen, M., de Ruysscher, D., Stalmans, W. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
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