Glutathione is one of the most abundant organic compounds found in many biological systems. It is a non-protein tripeptide of Glutamic acid, Cysteine and Glycine. Due to its stability, high cellular concentrations and structural features like gammaglutamyl linkage and sulfhydryl group, glutathione involves with many biological pathways including: cellular defense against xenobiotics and naturally occurring deleterious compounds, like free radicals, metal sequestering, and maintaining cellular sulfhydryl status. Glutathione has been broadly studied however the literature associated with Zn2+ coordination is not clear. This study is focused on collecting thermodynamic data of glutathione binding to Zn2+ metal ions using calorimetric technique. Isothermal titration calorimetry has been recommended as an excellent method to determine the association constant (K), enthalpy change (delta H), and binding stoichiometry (n) of a binding process. These parameters associated with Zn2+ binding glutathione deconvoluted from a series of complex equilibria provide an insight into what drives these reactions forward.
| Identifer | oai:union.ndltd.org:MSSTATE/oai:scholarsjunction.msstate.edu:td-5711 |
| Date | 11 December 2015 |
| Creators | Lakdusinghe, Madhubhashini |
| Publisher | Scholars Junction |
| Source Sets | Mississippi State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
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