Publication | Open Access
The ammonium sulfate activation of phosphorylase <i>b</i>
31
Citations
26
References
1990
Year
BiosynthesisEnzyme TetramerizationCellular EnzymologyBiochemistryAldo-keto ReductaseNatural SciencesEnzyme CatalysisGlycobiologyMolecular BiologyAmmonium Sulfate ActivationStructure-function Enzyme KineticsCellular BiochemistryChemical BiologyProteomicsAmmonium SulfateProtein Phosphorylation
The ammonium sulfate activation of phosphorylase b has been studied. Ammonium sulfate, when present in high concentrations, induces properties of phosphorylase a in phosphorylase b, such as an enhanced affinity for AMP, a reversal of the glucose-6-P inhibition and enzyme tetramerization. The data are consistent with the interpretation that sulfates bind to the Ser-14 site and the sulfate-protein interactions at this site are responsible for activation of phosphorylase b.
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