Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Purification and immunohistochemical tissue localization of human xanthine oxidase
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Preparation of the peroxisome proliferator-activated receptor α polyclonal antibody: Its application in fatty liver hemorrhagic syndrome
2021, International Journal of Biological MacromoleculesCitation Excerpt :At present, the structure and function of PPARα are relatively clear, but the preparation of anti-PPARα antibody has not been reported yet in Gallus. In the early days, the preparation of polyclonal antibodies in mammals is through the extraction of tissue protein, but the purified tissue protein was complex and unstable [35], which is difficult to meet the requirements of a single immunogen. The prokaryotic expression system can express a large number of target protein in a short time, and the target protein was easy to purify [36,37].
Prokaryotic expression of the chicken xanthine oxidase (XOD) subunit and its localization in liver and kidney
2016, International Journal of Biological MacromoleculesCitation Excerpt :Previous study reported that sometimes due to the hyperactivity of XOD occurred in the body, the by-products of both uric acid and ROS would play an important role in various pathophysiological conditions [4]. In work on mammals, the XOD proteins were always extracted and purified from the liver and milk to produce the polyclonal antibody for the further study of the relationship between the ischemia-reperfusion damage and the XOD [16–18]. The former studies of chicken XOD was also reported the way of extracted and purified XOD from liver for the study of the function and structure of the chicken XOD [1,19].
The cellular and molecular origin of reactive oxygen species generation during myocardial ischemia and reperfusion
2012, Pharmacology and TherapeuticsCitation Excerpt :These results contradict allopurinol-mediated free-radical reduction. Xanthine oxidase is readily expressed in endothelial cells that line the myocardial vasculature (Hellsten-Westing, 1993; Moriwaki et al., 1993), thus allopurinol may protect the myocardium by reducing post-ischemic O2•– production in endothelial cells. Alternatively, allopurinol has been shown to improve post-ischemic myocardial function independently of xanthine oxidase inhibition (Godin & Bhimji, 1987; Chambers et al., 1992; Hopson et al., 1995), an intrinsic antioxidant mechanism (Peterson et al., 1986) and cellular metabolic modulation (Ekelund et al., 1999; Cappola et al., 2001) have been proposed.
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