Date of Graduation
2002
Document Type
Thesis
Degree Type
MS
Committee Chair
Michael R. Gunther
Abstract
The pathogenesis of familial amyotrophic lateral sclerosis (fALS), a fatal neurodegenerative disease that sometimes results from SOD1 mutations, may involve the peroxidase reaction of the SOD1 protein. The aim of this thesis was to test the hypothesis that the peroxidase reaction of SOD results in SOD-centered peroxyl radical formation. The source of oxygen incorporated into 2-oxohistidine was to have been determined using HPLC/Mass spectrometry. This aim was not accomplished. UV-Visible difference spectrometry provided evidence for a peroxyl radical in this reaction. 2-oxohistidine formation was shown to be oxygen dependent and inhibited by the spin-trap MNP (Gunther, Peters, and Sivaneri 2002 JBC). The generation of free radicals is important in ALS, since free radical production results in cellular damage. The putative SOD peroxyl radical could contribute to oxidative cellular damage. Prevention of free radical generation might provide avenues for the treatment of ALS resulting from mutations with the SOD1 gene.
Recommended Citation
Peters, Joseph Andrew, "An investigation into the mechanism of 2-oxohistidine formation from the peroxidase activity of superoxide dismutase." (2002). Graduate Theses, Dissertations, and Problem Reports (ETD). 10675.
https://researchrepository.wvu.edu/etd/10675