Purification of Human γ-Glutamylcysteine Ligase Catalytic Subunit (GCLC)
dc.contributor.author | Ricketts, Daniel | |
dc.contributor.author | Haynes, Lindsey | |
dc.contributor.author | Martinez, Secilia | |
dc.contributor.author | Domfe, Jennifer | |
dc.contributor.author | Conrad-Webb, Heather | |
dc.contributor.author | Anderson, Mary E | |
dc.contributor.other | Anderson, Mary | |
dc.date.accessioned | 2021-03-20T00:19:26Z | |
dc.date.available | 2021-03-20T00:19:26Z | |
dc.date.issued | 2021 | |
dc.description | Creative Arts and Research Symposium | |
dc.description | Creative Arts and Research Symposium | en_US |
dc.description.abstract | Glutathione (GSH; L-γ-glutamyl-L-cysteinylglycine), an intracellular antioxidant, has multiple important roles including, cellular protection against reactive oxygen species, oxidative stress, and toxic compounds. Low GSH is associated with a number of diseases. Biosynthesis of GSH is catalyzed by two ATP-dependent enzymes, γ-Glutamylcysteine ligase (GCL) and glutathione synthetase. While these enzyme’s activities are known, their regulation are not well understood, in part because of difficulty in purification, especially of the catalytic subunit of GCL (GCLC). Our goal is to improve purification of human GCLC, by modifying chromatography and induction parameters (i.e. temperature of induction, time of induction and/or amount of inducing agent.) so GSH synthesis can be studied. Supported by the Department of Chemistry and Biochemistry Welch Grant. | |
dc.description.department | Chemistry & Biochemistry | |
dc.description.sponsorship | Robert A. Welch Foundation | |
dc.identifier.uri | https://hdl.handle.net/11274/12921 | |
dc.language.iso | en_US | en_US |
dc.title | Purification of Human γ-Glutamylcysteine Ligase Catalytic Subunit (GCLC) | en_US |
dc.type | Poster | en_US |
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