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Volume 271, Number 44, Issue of November 1, 1996 pp. 27569-27574
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Thermodynamic Characterization of 5'-AMP Binding to Bovine Liver Glycogen Phosphorylase a

(Received for publication, June 18, 1996, and in revised form, July 29, 1996)

Luis García-Fuentes Dagger , Ana Cámara-Artigas Dagger , Obdulio López-Mayorga § and Carmen Barón Dagger

From the Dagger  Departamento de Química Física, Bioquímica y Química Inorgánica, Facultad de Ciencias Experimentales, Universidad de Almería, Almería, Spain and § Instituto de Biotecnología de la Universidad de Granada, Granada, Spain

The binding of adenosine 5'-monophosphate to liver glycogen phosphorylase a (EC 2.4.1.1) has been studied by size exclusion high performance liquid chromatography and isothermal titration microcalorimetry at pH 6.9 over a temperature range of 25 to 35 °C. The results are compared with those of the binding of the same nucleotide to the muscle isozyme and to liver phosphorylase b. Calorimetric measurements in various buffer systems with different ionization heats suggest that protons are released during the binding of the nucleotide. The dimer of liver glycogen phosphorylase a has been shown to have two equal and independent sites for 5'-AMP, which would correspond to the activator sites identified in the muscle isozyme. The binding constants as well as the changes in Gibbs energy, enthalpy, and entropy per site for 5'-AMP binding were calculated at each temperature. The results show that the major contribution to the negative value of Delta G0 stems from the value of Delta H in the range of 25 to 35 °C. The enthalpy change of binding is strongly temperature-dependent, arising from a large negative Delta Cp of binding equal to -1.45 ± 0.02 kJ K-1 (mol of 5'-AMP bound)-1, which suggests significant changes in the polar and apolar surfaces accessible to the solvent.


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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.