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- Park, Sunghoon
- Biochemical Engineering Lab.
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Purification and characterization of human caseinomacropeptide produced by a recombinant Saccharomyces cerevisiae
- Author(s)
- Kim, Yu-Jin, Park, Sunghoon, Oh, You-Kwan, Kang, Whankoo, Kim, Hee Sook, Lee, Eun Yeol
- Issued Date
- 2005-06
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, v.41, no.2, pp.441 - 446
- Abstract
- Caseinomacropeptide (CMP) is a biologically active polypeptide derived from the C-terminal Of milk K-casein. CMP is heterogeneous since it is modified differently by glycosylation and phosphorylation after translation. Recently, recombinant human CMP (hCMP) has been produced as a secretory product in yeast. The present Study aimed at the purification and characterization of recombinant hCMP. By sequential molecular cut-off ultrafiltration and anion-exchange chromatography, the recombinant hCMP in the culture broth could be purified to an HPLC purity over 94 %. The authenticity of the purified hCMP was confirmed by sequence analysis of N-terminal amino acids. The recombinant hCMP was estimated to be 7.0 kDa by SDS-PAGE, and showed a lower glycosylation than the natural bovine CMP.
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- ISSN
- 1046-5928
- Keyword (Author)
- Caseinomacropeptide, Saccharomyces cerevisiae, ultrafiltration, anion-exchange chromatography, O-glycosylation
- Keyword
- CASEIN MACROPEPTIDE, O-GLYCOSYLATION, K-CASEIN, GLYCOMACROPEPTIDE, GROWTH, YEAST, CELLS, RAT
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