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Title: On the mechanism of hepatic glycogenolysis induced by anoxia or cyanide. Author: Bollen M, de Ruysscher D, Stalmans W. Journal: Biochem Biophys Res Commun; 1983 Sep 30; 115(3):1033-9. PubMed ID: 6626215. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]