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Circular Dichroism studies on the aromatic residues of fructose 1, 6-Bisphosphatase from Turkey liver

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.

Identiferoai:union.ndltd.org:auctr.edu/oai:digitalcommons.auctr.edu:dissertations-4831
Date01 August 1976
CreatorsOgoe, Samuel A.
PublisherDigitalCommons@Robert W. Woodruff Library, Atlanta University Center
Source SetsAtlanta University Center
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceETD Collection for AUC Robert W. Woodruff Library

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