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dc.contributor.advisorPregenzer, Jeff
dc.contributor.authorBooth, Sarah
dc.description1 broadside : ill.
dc.description.abstractGlutathione (GSH) is a powerful antioxidant that prevents cell toxicity through conjugation to harmful reactive intermediaries and foreign compounds. The reaction is catalyzed by glutathione S-transferase (GST). GSH can be depleted after the metabolism of pharmaceutical drugs. Because maintaining GSH concentration in cells is vitally important, the effect that candidate drugs have on GSH levels is assessed in preliminary stages of drug development. The GSH-monochlorobimane (mBCl) assay has been developed to measure GSH reduction after the metabolism of compounds by cytochrome P450 enzymes (CYP450s) in human and rat microsomes. Controls of 1-aminobenzotriazole (+ABT) are used to assure that the drug was metabolized by CYP450s. NADPH was used to keep GSH in the active reduced form; a negative NAPDH control was used as well (NADPH). Early assays with human microsomes had large GSH reductions, caused by the microsomes themselves. This study aimed to mediate that reduction, producing a viable assay to assess new compounds’ toxicity.
dc.description.sponsorshipCeeTox, Kalamazoo, MI
dc.description.sponsorshipKalamazoo College. Department of Biology. Diebold Symposium, 2007
dc.description.tableofcontentsIntroduction -- Materials and methods -- Results -- Conclusions
dc.titleIn GSH-mBCI Assay, Increased GSH Concentration and Pre-Incubation with NADPH and ABT Overcomes Signal Reductionen

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  • Diebold Symposium Posters and Schedules [479]
    Poster and oral presentations by senior biology majors that include the results of their Senior Integrated Projects (SIPs) at the Diebold Symposium. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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