摘要
Human ceruloplasmin (Cp) has been purified from cryoprecipitate-poor plasma as a by-product of the C1-inhibitor production chain. Highly purified Cp was obtained by subsequent ion-exchange chromatography on sulfate-Fractogel EMD and TMAE-Fractogel EMD. Treatments for viral safety included application of the solvent-detergent method and two nanofiltration steps using 35- and 15-nm pore size filters at the end of the process. Overall antigen yield was 95 (±5)%. Purified human ceruloplasmin was studied by electron spin resonance (ESR) to characterize its different types of copper complexes and to check its antioxidant properties. We distinguished three types of complexes: One type-2 Cu(II) with g//=2.25 and A//=180 G and two type-1 Cu(II) exhibiting different narrow hyperfine splitting (A//=72 G and A//=90 G) with close g//(2.20 and 2.21). Purified Cp has a specific activity of 24.5±0.2 mU/mg of proteins. This process provides a method for Cp purification that could be easily integrated into modern plasma fractionation.
原文 | 英語 |
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頁(從 - 到) | 1406-1409 |
頁數 | 4 |
期刊 | Biological and Pharmaceutical Bulletin |
卷 | 23 |
發行號 | 12 |
出版狀態 | 已發佈 - 2000 |
對外發佈 | 是 |
ASJC Scopus subject areas
- 分子醫學
- 藥理學、毒理學和藥劑學 (全部)