TY - JOUR JF - sjimu JO - J. Ilam Uni. Med. Sci. VL - 20 IS - 4 PY - 2013 Y1 - 2013/2/01 TI - Purification of Ferritin From Sheep Liver and The Report of Peroxidase Activity of Heme-Ferritin Complex TT - تخلیص فریتین از کبد گوسفند و گزارش فعالیت پراکسیدازی مجموعه هیم-فریتین N2 - 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. SP - 117 EP - 126 AU - Ranjbar, s AU - Jaafari, m AU - Khodarahmi, r AU - Zarei, z AU - Ashrafi, mr AU - Miraghaei, s sh AD - KW - ferritin KW - purification KW - anion exchange chromatography KW - peroxidase acti-ity UR - http://sjimu.medilam.ac.ir/article-1-877-en.html ER -