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This paper briefly explores the xanthine oxidase enzyme, its impact upon the body, and the research which has explored how and why this enzyme functions. The writer discusses that due to the easy accessibility of xanthine oxidase in cow's milk, this enzyme has been the subject of numerous studies for more than a century. However, the writer points out that despite this heavy level of scrutiny, xanthine oxidase is still not fully understood. This paper explores the literature which reflects upon past studies into xanthine oxidase and current research and potential applications for this substance.
From the Paper:"The basic construction of xanthine oxidase has been extensively documented and is understood: This enzyme functions as a dehydrogenase which converts hypoxanthine to xanthine, and converts xanthine into uric acid. The conversion of hypoxanthine to xanthine alters the hypoxanthine, a purine, into a degraded purine, which then is further degraded into uric acid which is then passed from the system. Granell et al stress that: Under [normal] physiologic conditions, the enzyme exists mainly as xanthine dehydrogenase (XDH), a form that uses NAD^+ as electron acceptor. Nevertheless, under certain circumstances, XDH can be converted to xanthine oxidase (XOD) by limited proteolytic cleavage. XOD uses molecular oxygen as electron acceptor and consequently generates the superoxide anion, a molecule that participates in the generation of other reactive oxygen species including hydrogen peroxide, hydroxyl radical and peroxynitrite."
Cite this Essay:
Xanthine Oxidase (2005, December 01) Retrieved May 25, 2020, from https://www.academon.com/essay/xanthine-oxidase-84172/
"Xanthine Oxidase " 01 December 2005. Web. 25 May. 2020. <https://www.academon.com/essay/xanthine-oxidase-84172/>