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Nucleic Acids Research, 1985, Vol. 13, No. 4 1151-1162
© 1985

Articles

Efficient secretion and purification of human insulin-like growth factor I with a gene fusion vector in Staphylococci

Björn Nilsson, Erik Holmgren1, Staffan Josephson1, Sten Gatenbeck, Lennart Philipson2,* and Mathias Uhlen

Department of Biochemistry and Biotechnology, Royal Institute of Technology S-100 44 Stockholm 1KabiGen Ltd. S-112 87 Stockholm, sweden 2European Molecular Biology Laboratory Postfach 10.2209, 6900 Heidelberg 1, FRG

To whom correspondence should be addressed

Received December 10, 1984. Revised January 23, 1985. Accepted January 23, 1985.

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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