COMPARATIVE CHARACTERIZATION OF LIVER-GLYCOGEN METABOLISM IN RAT AND GUINEA-PIG

B TOTH*, D ZELENA, K SZUCS, B SZOOR, P GERGELY

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 Ca2+-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-I is phosphorylated by cyclic AMP-dependent protein kinase.

Original languageEnglish
Pages (from-to)547-552
Number of pages6
JournalComparative Biochemistry and Physiology Part B: Comparative Biochemistry
Volume103
Issue number3
Publication statusPublished - Nov 1992

Keywords / Materials (for Non-textual outputs)

  • RABBIT SKELETAL-MUSCLE
  • PROTEIN PHOSPHATASES
  • PHOSPHORYLASE-PHOSPHATASE
  • HORMONAL-REGULATION
  • SPONGE TOXIN
  • OKADAIC ACID
  • KINASE
  • QUANTITATION
  • STIMULATION
  • INHIBITOR-1

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