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- W90489477 endingPage "160" @default.
- W90489477 startingPage "89" @default.
- W90489477 abstract "This chapter discusses the molecular details of the regulation of the system of enzymes involved in the breakdown of glycogen to produce glucose 1-phosphate, one of the entry points into glycolysis in rabbit skeletal muscle. As phosphorylase is an enzyme of large molecular weight (2.0 × 105 for the more common active dimeric form), structural studies present considerable difficulties. This has been complicated by the fact that the most common crystal form of the enzyme contained the tetramer, which is the predominant form for phosphorylase a and the b form in the presence of AMP at high concentrations of enzyme. Proteolysis by trypsin of phosphorylase a results in a cleavage of the amino end of the molecule—the resulting hexapeptide contains the serine residue that is phosphorylated in the kinase-catalyzed phosphorylation of the enzyme and is rich in basic amino acids. Phosphorylase Kinase enzyme is responsible for phosphorylation of phosphorylase b." @default.
- W90489477 created "2016-06-24" @default.
- W90489477 creator A5040554416 @default.
- W90489477 creator A5042124702 @default.
- W90489477 date "1976-01-01" @default.
- W90489477 modified "2023-10-15" @default.
- W90489477 title "Regulation of the Glycogen Phosphorylase System—From Physical Measurements to Biological Speculations" @default.
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