Showing papers by "Pál Gergely published in 1980"
TL;DR: 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.
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.
1 citations
TL;DR: Phosphorylase b ′, a modified form of phosphorylases a in which the phosphorylated site has been removed by tryptic attack, can increase the liberation of 32 P from the tetradecapeptide.