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KMID : 0043320090320050693
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Archives of Pharmacal Research
2009 Volume.32 No. 5 p.693 ~ p.698
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A Novel and One-step Purification of Human Ceruloplasmin by Acharan Sulfate Affinity Chromatography
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Kim Yeong-Shik
Hahn Bum-Soo
Joo Eun-Ji
Lee In-Sun
Park You-Mie
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Abstract
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Human ceruloplasmin, a copper binding α2-glycoprotein, was purified by a single-step procedure using acharan sulfate affinity chromatography. Acharan sulfate was immobilized to aminefunctionalized 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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KEYWORD
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Acharan sulfate, Affinity chromatography, Copper binding α2-glycoprotein, Human ceruloplasmin, Protein purification
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