Abstract
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.
MeSH terms
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Adenosine Monophosphate / pharmacology
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Ammonium Sulfate / pharmacology*
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Animals
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Electron Spin Resonance Spectroscopy
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Enzyme Activation / drug effects
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Glucosephosphates / metabolism
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Kinetics
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Macromolecular Substances
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Muscles / enzymology*
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Phosphorylase b / metabolism*
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Phosphorylases / metabolism*
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Rabbits
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Ultracentrifugation
Substances
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Glucosephosphates
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Macromolecular Substances
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Adenosine Monophosphate
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glucose-1-phosphate
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Phosphorylase b
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Phosphorylases
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Ammonium Sulfate