Abstract
Human ceruloplasmin, a copper binding α2-glycoprotein, was purified by a single-step procedure using acharan sulfate affinity chromatography. Acharan sulfate was immobilized to amine-functionalized agarose matrix through carboxylic acids. Ceruloplasmin in human plasma was obtained from 0.4 M NaCl salt elution and characterized by SDS-PAGE (132 and 125 kDa), isoelectric focusing (pI 4.6), Western blotting, and MALDI-TOF-MS peptide mass fingerprinting. Ceruloplasmin was purified 106 fold with a specific oxidase activity of 0.53 U/mg protein.
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Park, Y., Lee, I.S., Joo, E.J. et al. A novel and one-step purification of human ceruloplasmin by acharan sulfate affinity chromatography. Arch. Pharm. Res. 32, 693–698 (2009). https://doi.org/10.1007/s12272-009-1507-4
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DOI: https://doi.org/10.1007/s12272-009-1507-4