Multiple phosphorylation of rabbit skeletal muscle glycogen synthase. Evidence for interactions among phosphorylation sites and the resolution of electrophoretically distinct forms of the subunit

Phosphorylation of rabbit skeletal muscle glycogen synthase by a cyclic nucleotide and Ca2+-independent protein kinase, PC0.7, caused the enzyme to be a better substrate for phosphorylation by another cyclic nucleotide and Ca2+-independent protein kinase, FA/GSK-3. In contrast, phosphorylation by th...

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Veröffentlicht in:	The Journal of biological chemistry 1983-09, Vol.258 (17), p.10702-10709
Hauptverfasser:	DePaoli-Roach, A A, Ahmad, Z, Camici, M, Lawrence, J C, Roach, P J
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cyclic AMP - metabolism Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glycogen Synthase - metabolism Ligases Macromolecular Substances Muscles - enzymology Phosphorylation Protein Kinases - metabolism Rabbits
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