Format

Send to

Choose Destination
Nucleic Acids Res. 1985 Feb 25;13(4):1151-62.

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

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.

PMID:
3889837
PMCID:
PMC341062
DOI:
10.1093/nar/13.4.1151
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Silverchair Information Systems Icon for PubMed Central
Loading ...
Support Center