Tryptophan fluorescence studies on turkey liver fructose 1,6-bisphosphatase, 1976

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Title: Tryptophan fluorescence studies on turkey liver fructose 1,6-bisphosphatase, 1976
Author: Quinsey, Carmen Denise
Decade: 1970-1979
Abstract: 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.
Document Type: text
Format: application/pdf
Date of Award: 1976-12-01
Degree Type: thesis
Degree Name: Master of Science (MS)
Granting Institution: Atlanta University
Department: Chemistry
Advisor: Owen, G. Scott
Johnson, Joe
Institution: Clark Atlanta University
Geographic Location: Georgia--Atlanta
Handle: http://hdl.handle.net/20.500.12322/cau.td:1976_quinsey_carmen_d