Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency
Francis GL, Ross M, Ballard FJ, et al. Journal of Molecular Endocrinology 1992;8:213-223.
What it found
Described how Long IGF-I, Long [Gly3]-IGF-I and Long [Arg3]-IGF-I (LR3) were produced in E. coli: IGF-1 with an N-terminal extension from pig growth hormone, plus a substitution at position 3. In rat muscle cells and other cells that release IGF-binding proteins, all analogues were more potent than IGF-1, with Long [Arg3]-IGF-I among the most potent. In chick cells without binding proteins, Long [Arg3]-IGF-I was less potent than IGF-1.
Limitations
Cells only. Shows how the molecule behaves in culture, not in a living body.
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