Date of Award

12-1-1976

Degree Type

Thesis

University or Center

Atlanta University (AU)

Degree Name

M.S.

Department

Chemistry

First Advisor

Dr. G. Scott Owen

Second Advisor

Dr. Joe Johnson Jr.

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.

Included in

Chemistry Commons

Share

COinS