Abstract
Protein-protein interactions detected in tissue extracts, or between purified protein preparations, and also in a protein-glycogen complex have a crucial role in the regulation of glycogen metabolism through phosphorylation-dephosphorylation processes. Interactions between phosphoprotein phosphatase and phosphorylase kinase, cAMP-dependent protein kinase and other protein-like inhibitors controlling the dephosphorylation reactions are reviewed in our paper, and a possible sequence of dephosphorylation is suggested to describe the correlated events taking place in a cell.
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