AU - Ranjbar, s AU - Jaafari, m AU - Khodarahmi, r AU - Zarei, z AU - Ashrafi, mr AU - Miraghaei, s sh TI - Purification of Ferritin From Sheep Liver and The Report of Peroxidase Activity of Heme-Ferritin Complex PT - JOURNAL ARTICLE TA - sjimu JN - sjimu VO - 20 VI - 4 IP - 4 4099 - http://sjimu.medilam.ac.ir/article-1-877-en.html 4100 - http://sjimu.medilam.ac.ir/article-1-877-en.pdf SO - sjimu 4 AB  - Introduction: Ferritin (with molecular weight: 450 kDa, 24 subunits) is composed of light and heavy chains and has a major role in circulating iron storage, so that up to 4500 ferric iron ions (Fe3+) can be stored within its structure. The aim of this study was purification of ferritin from liver (the tissue that contains large amounts of ferritin) with high yield/purity, and evalu-ation of its possible peroxidase activity. Materials & Methods: For successful purification of ferritin, we employed the obvious characteristic of ferritin (high ther-mal resistance against temperatures over 80°C) in two steps accompanying with ammonium sulfate precipitation and anionic exchange chromatography (DEAE-cellul-ose). Findings: Ferritin was successfully purified and its purity (~ 95%) was confirmed using SDS-PAGE. Also at the present study, the peroxidase activity of heme-ferritin com-plex for the first time is documented. Discussion & Conclusion: Since ferritin is widely used in diagnosis as well as research fields, its purification is inevitable prereq-uisite. Oxidative stress, as the main cause of neurodegenerative diseases, may also corre-late with increased concentrations of ferritin in AD brain. CP - IRAN IN - LG - eng PB - sjimu PG - 117 PT - Research YR - 2013