Circular Dichroism studies on the aromatic residues of fructose 1, 6-Bisphosphatase from Turkey liver, 1976
Ogoe, Samuel A.
1970-1979
This thesis presents a detailed description and analysis of the circular dichroism studies performed on the aromatic residues of fructose 1, 6-bisphosphatase (FbPase) from turkey liver under various experimental conditions. Circular dichroism studies performed on the aromatic residues of FbPase indicate that the presence of the substrate, fructose 1, 6-bisphosphate (FbP) and/or the allosteric inhibitor, adenosine monophosphate (AMP) 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, on the conformation of the enzyme is more pronounced than that of the substrate, FbP.
text
application/pdf
1976-08-01
thesis
Master of Science (MS)
Atlanta University
Chemistry
Clark Atlanta University
Georgia--Atlanta
http://hdl.handle.net/20.500.12322/cau.td:1976_ogoe_samuel_a