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  • Title: Production, purification, and characterization of rat pro-CCK from serum-free adapted Drosophila cells.
    Author: Kleditzsch P, Pratt J, Vishnuvardhan D, Henklein P, Schade R, Beinfeld MC.
    Journal: Protein Expr Purif; 2003 Sep; 31(1):56-63. PubMed ID: 12963341.
    Abstract:
    The precursor of cholecystokinin (pro-CCK) was expressed and purified from media of stably transfected D.Mel-2 cell as an V5-His tagged fusion protein. Its identity was confirmed using SDS-PAGE, immunoblotting, gel filtration chromatography, HPLC, and Mass Spectroscopy. Two major forms of pro-CCK were found with a molecular weight of about 14.4 and 11.3 kDa. The smaller form represents the V5-His tagged pro-CCK after cleavage at a single arginine residue at CCK-58. This cleavage is probably being performed by endogenous proteases in these cells. Purification of the desired larger form of pro-CCK is possible using a nickel column with a recovery of about 20%, yielding 500 microg/L media. The purified protein is stable for several months and can be used for further functional studies of pro-CCK.
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