Abstract
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.
Original language | English |
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Pages (from-to) | 1406-1409 |
Number of pages | 4 |
Journal | Biological and Pharmaceutical Bulletin |
Volume | 23 |
Issue number | 12 |
Publication status | Published - 2000 |
Externally published | Yes |
Keywords
- Antioxidant
- Ceruloplasmin
- ESR spectroscopy
- Reactive oxygen specie
ASJC Scopus subject areas
- Molecular Medicine
- Pharmacology, Toxicology and Pharmaceutics(all)