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Efficient secretion and purification of human insulin-like growth factor I with a gene fusion vector in Staphylococci.
Authors:B Nilsson   E Holmgren   S Josephson   S Gatenbeck   L Philipson     M Uhlen
Abstract:A novel approach for production of small polypeptides, using a staphylococcal protein A vector, is described. This system is used to express, secrete and purify human insulin-like growth factor I (IGF-I). A fusion protein consisting of protein A and IGF-I is recovered in high yield by passing the culture medium through an IgG affinity column. Using site-specific mutagenesis an acid labile asp-pro cleavage site was introduced at the fusion point between the two proteins. The protein A "tail" can thereby be removed from the affinity purified fusion protein by chemical cleavage releasing biologically active IGF-I molecules.
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