:: Volume 20, Issue 4 (2-2013) ::
sjimu 2013, 20(4): 117-126 Back to browse issues page
Purification of Ferritin From Sheep Liver and The Report of Peroxidase Activity of Heme-Ferritin Complex
S Ranjbar, M Jaafari, R Khodarahmi 1, Z Zarei, Mr Ashrafi, S sh Miraghaei
1- , rkhodarahmi@mbrc.ac.ir
Abstract:   (9062 Views)
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.
Keywords: ferritin, purification, anion exchange chromatography, peroxidase acti-ity
Full-Text [PDF 534 kb]   (1927 Downloads)    
Type of Study: Research | Subject: exclusive bacteriology
Received: 2013/02/20 | Accepted: 2013/03/17 | Published: 2013/03/17


XML   Persian Abstract   Print



Volume 20, Issue 4 (2-2013) Back to browse issues page