Purification of Human Ceruloplasmin as a By-Product of C1-Inhibitor.

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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 precess. 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.

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