Comparative characterization of liver glycogen metabolism in rat and guinea-pig.
1. Guinea-pig liver contained more phosphorylase in the active (phosphorylated) form and less synthase in the active (dephosphorylated) form when compared with rat liver. 2. Activities of cyclic AMP-dependent protein kinase and Ca(2+)-dependent phosphorylase kinase were the same in rat and guinea-pig livers. 3. Activities of phosphorylase phosphatase and synthase phosphatase in the extract and glycogen plus microsomal fraction of guinea-pig liver were significantly lower than those of rat liver. 4. The existence of inhibitor-1 in the liver of guinea-pig can maintain a lower activity of type-1 protein phosphatase, especially when inhibitor-1 is phosphorylated by cyclic AMP-dependent protein kinase.
Tóth
B
B
Department of Medical Chemistry, University School of Medicine, Debrecen, Hungary.
Zelena
D
D
Szücs
K
K
Szöör
B
B
Gergely
P
P
D000818:Animals; D006006:Glycogen Synthase / Q000378:metabolism; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008112:Liver Glycogen / Q000378:metabolism*; D008297:Male; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism; D006005:Phosphorylases / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013045:Species Specificity; D013347:Subcellular Fractions / Q000378:metabolism
D008112:Liver Glycogen; D006005:Phosphorylases; D006006:Glycogen Synthase; D010765:Phosphorylase Phosphatase