Comparison of enzyme activities on glycogen metabolism in rabbit slow and fast muscles
- PMID: 2992876
- DOI: 10.1016/0305-0491(85)90379-7
Comparison of enzyme activities on glycogen metabolism in rabbit slow and fast muscles
Abstract
Activities of glycogen synthase (total) and branching enzyme in slow (soleus) muscle are higher than those in fast (vastus lateralis) muscle, while those of phosphorylase kinase (total), phosphorylase (total) and debranching enzyme are reversed. The active form ratio of glycogen synthase is higher in fast muscle, while those of phosphorylase kinase and phosphorylase are higher in slow muscle. Activities of cAMP-dependent protein kinase and protein phosphatase in slow muscle are higher than those in fast muscle. These results suggest that glycogen metabolizing enzymes in slow muscle, distinct from those in fast muscle, are regulated more strongly by cAMP-dependent protein kinase rather than by protein phosphatase.
Similar articles
-
Dephosphorylation of skeletal muscle phosphorylase, glycogen synthase, and phosphorylase kinase beta-subunit by a Mn2+-activated protein phosphatase.Arch Biochem Biophys. 1982 Nov;219(1):228-35. doi: 10.1016/0003-9861(82)90153-9. Arch Biochem Biophys. 1982. PMID: 6295283 No abstract available.
-
Purification of muscle glycogen particles by glycerol-gradient centrifugation.FEBS Lett. 1977 Sep 1;81(1):166-72. doi: 10.1016/0014-5793(77)80952-6. FEBS Lett. 1977. PMID: 409620 No abstract available.
-
Effect of immobilization on the enzymes of glycogen metabolism.Acta Physiol Hung. 1983;62(1):85-91. Acta Physiol Hung. 1983. PMID: 6417977
-
Enzymatic control of glycogen degradation in smooth muscle.Prog Clin Biol Res. 1988;259:391-411. Prog Clin Biol Res. 1988. PMID: 2834743 Review. No abstract available.
-
The substrate specificity and regulation of the protein phosphatases involved in the control of glycogen metabolism in mammalian skeletal muscle.Adv Enzyme Regul. 1977 Oct 3-4;16:97-119. doi: 10.1016/0065-2571(78)90069-9. Adv Enzyme Regul. 1977. PMID: 211821 Review. No abstract available.