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An efficient expression system in Escherichia coli for several biologically active insulin-like growth factor-I (IGF-I) fusion peptide analogues is described. These novel IGF-I fusion protein(More)
Insulin-like growth factor-1 (IGF-1), whether recombinant, chemically-synthesised or purified from bovine colostrum, was equipotent in radioreceptor assays with IGF-1 or insulin-like growth factor-2(More)
We have investigated insulin-like growth factor (IGF)-I and IGF-II binding to bovine insulin-like growth factor binding protein-2 (bIGFBP-2) using chemical modification to locate sites on the IGF(More)
The development of an efficient expression system for insulin-like growth factor-I (IGF-I) in Escherichia coli as a fusion protein is described. The fusion protein consists of an N-terminal extension(More)