A novel and one-step purification of human ceruloplasmin by acharan sulfate affinity chromatography |
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| Authors: | Youmie Park In Sun Lee Eun Ji Joo Bum-Soo Hahn Yeong Shik Kim |
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| Institution: | (1) Natural Products Research Institute, College of Pharmacy, Seoul National University, Seoul, 151-742, Korea;(2) National Academy of Agricultural Science, Suwon, 441-857, Korea |
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| 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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| Keywords: | Acharan sulfate Affinity chromatography Copper binding α 2-glycoprotein Human ceruloplasmin Protein purification |
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