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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and characterization of human caseinomacropeptide produced by a recombinant Saccharomyces cerevisiae.

Caseinomacropeptide (CMP) is a biologically active polypeptide derived from the C-terminal of milk kappa-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 7.0kDa by SDS-PAGE, and showed a lower glycosylation than the natural bovine CMP.[1]

References

  1. Purification and characterization of human caseinomacropeptide produced by a recombinant Saccharomyces cerevisiae. Kim, Y.J., Park, S., Oh, Y.K., Kang, W., Kim, H.S., Lee, E.Y. Protein Expr. Purif. (2005) [Pubmed]
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