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The allosteric transition of glycogen phosphorylase

✍ Scribed by Barford, D.; Johnson, L. N.

Book ID
109760858
Publisher
Nature Publishing Group
Year
1989
Tongue
English
Weight
833 KB
Volume
340
Category
Article
ISSN
0028-0836

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πŸ“œ SIMILAR VOLUMES

Alteration of the intramolecular dynamic
Alteration of the intramolecular dynamics of glycogen phosphorylase b by allosteric ligands
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Phosphorylase 6 (E.C. 2.4.1.1), prepared from rabbit skeletal muscle, was used to study whether the binding of allosteric ligands modifies the intramolecular dynamics of the protein matrix. Protein dynamics were monitored through the fluorescence and phosphorescence parameters of the 12 tryptophan (

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Kinetic analysis and modelling of the allosteric behaviour of liver and muscle glycogen phosphorylases
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Allosteric enzymes have very complex kinetic behaviours which are primarily interpreted through simplified models. To describe the functional properties of liver and muscle glycogen phosphorylase isozymes we have developed an experimental strategy based on the measurements of initial reaction rates