Tryptophan fluorescence studies on turkey liver fructose 1,6-bisphosphatase, 1976
Quinsey, Carmen Denise
1970-1979
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.
text
application/pdf
1976-12-01
thesis
Master of Science (MS)
Atlanta University
Chemistry
Owen, G. Scott Johnson, Joe
Clark Atlanta University
Georgia--Atlanta
http://hdl.handle.net/20.500.12322/cau.td:1976_quinsey_carmen_d