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dc.contributor.advisorAnderson, Mary E
dc.creatorStopper, Anna Rachel
dc.date.accessioned2020-02-24T15:20:54Z
dc.date.available2020-02-24T15:20:54Z
dc.date.created2018-12
dc.date.issued2019-03-04
dc.date.submittedDecember 2018
dc.identifier.urihttps://hdl.handle.net/11274/12176
dc.description.abstractGlutathione (GSH) is a tripeptide important in preventing cellular oxidative damage. Human glutathione synthetase (hGS) catalyzes the second stage of GSH biosynthesis. Homodimeric human glutathione synthetase is negatively cooperative with respect to its L-γ-Glu-Cys substrate. Although the allosteric effects of substrates binding to hGS have been studied, the order of substrate binding has not. GS in plants and prokaryotes are reported to exhibit opposing random ter and ordered ter ter reaction orders respectively; currently little is known about the reaction order in humans. Knowledge of the mechanism and reaction order of hGS is vital to understand how it contributes to the regulation of the levels of the limiting amino acid cysteine and of glutathione. Using ITC binding studies the mechanism of action and reaction order of hGS has been evaluated and suggests a semi-ordered reaction in human GS.
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.subjectHuman glutathione synthetase
dc.subjectIsothermal titration calorimetry
dc.subjectEnzyme
dc.subjectBinding
dc.subjectReaction order
dc.subjectCheck points
dc.subjectRegulation
dc.subjectITC
dc.titleHuman glutathione synthetase reaction order and kinetics examined using spectroscopic and calorimeteric techniques
dc.typeThesis
dc.date.updated2020-02-24T15:20:54Z
thesis.degree.departmentChemistry and Biochemistry
thesis.degree.disciplineChemistry
thesis.degree.grantorTexas Woman's University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science
dc.type.materialtext
dc.creator.orcid0000-0003-2271-9377


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