Abstract
The generality of the covalent phosphorylation of glycogen synthase was established. The stoichiometry of the complete conversion of the rabbit skeletal muscle enzyme was worked out. The identity of the hexapeptide sequence of the phosphorylated site in muscle glycogen synthase and phosphorylase was reestablished. The electron microscopy of the enzyme was studied. Synthase kinase was demonstrated to be a site of hormonal control in muscle and in liver. A set of equations has been written to delineate the enzymatic cascade of insulin stimulated glycogen synthesis.
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© 1974 Springer-Verlag Berlin · Heidelberg
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Larner, J. et al. (1974). Studies on Glycogen Synthase and Its Control by Hormones. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_7
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DOI: https://doi.org/10.1007/978-3-642-80817-3_7
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