Date of Award
Department of Chemistry
G. S. Owen
The purpose of this thesis is to give a description and analysis of circular dichroism studies of the secondary structure of both the native and alkaline forms of chicken liver fructose 1,6-bisphosphatase (FbPase). The conformation studies of the enzyme are performed by examining changes in the secondary structure, when the substrate, fructose 1,6-bisphosphate (FbP), and/or the allosteric inhibitor, adenosine 5'-monophosphate (AMP), bind to the enzyme, at pH 7 and 9. Previous studies of FbPase from turkey liver indicate that the presence of the substrate and/ or the inhibitor, as well as changes in the pH of the medium, produce significant effects on the conformation of the enzyme. The effect of the inhibitor, AMP, is more pronounced than that of the substrate, FbP.
Mensah, Isaac T., "Circular dichroism studies on the secondary structure of the native and the alkaline forms of fructose 1,6-bisphosphatase from chicken liver" (1979). ETD Collection for AUC Robert W. Woodruff Library. 3419.