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Purification of Ferritin From Sheep Liver and The Report of Peroxidase Activity of Heme-Ferritin Complex
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S Ranjbar   , M Jaafari , R Khodarahmi * 1, Z Zarei , Mr Ashrafi , S sh Miraghaei |
| 1- , rkhodarahmi@mbrc.ac.ir |
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Abstract: (11024 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. |
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| Keywords: ferritin, purification, anion exchange chromatography, peroxidase acti-ity |
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Full-Text [PDF 534 kb]
(3144 Downloads)
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Type of Study: Research |
Subject:
exclusive bacteriology
Received: 2013/02/20 | Accepted: 2013/03/17 | Published: 2013/03/17
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