The native form of turkey liver fructose 1,6-bisphosphatase (FbPase) consists of four identical subunits, each of which contains one tryptophan residue. The fluorescence emission spectra of the tryptophan residues have been recorded as a function of changes in pH, substrate (fructose 1,6-bisphosphate) and inhibitor (adenosine-5’ monophosphate) binding, and the addition of the metal cofactors Mg+2, Mn+2 and Co+2 . Changes in the fluorescence emission spectra of the tryptophan residues indicate that conformational changes in the enzyme occur under the above conditions.
Identifer | oai:union.ndltd.org:auctr.edu/oai:digitalcommons.auctr.edu:dissertations-4561 |
Date | 01 December 1976 |
Creators | Quinsey, Carmen Denise |
Publisher | DigitalCommons@Robert W. Woodruff Library, Atlanta University Center |
Source Sets | Atlanta University Center |
Detected Language | English |
Type | text |
Format | application/pdf |
Source | ETD Collection for AUC Robert W. Woodruff Library |
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