Clinical Chemistry
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Clinical Chemistry 33: 544-548, 1987;
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Clinical Chemistry, Vol 33, 544-548, Copyright © 1987 by American Association for Clinical Chemistry

Natural and recombinant DNA-derived human insulin-like growth factor-I compared for use in radioligand assays

RC Baxter, JS De Mellow and BD Burleigh

We compared two preparations of human insulin-like growth factor (IGF)- I, one isolated from human plasma and the other prepared by recombinant DNA technology, for use in three radioimmunoassays and a radioreceptor assay for IGF-I, two radioreceptor assays for IGF-II, and a protein- binding assay for both IGFs. In the IGF-I assays, iodinated natural IGF- I consistently showed higher binding than did iodinated biosynthetic IGF-I, whether or not the iodopeptides were purified before use by hydrophobic interaction chromatography. Comparing the potency of the unlabeled peptides in the eight assay systems, we found the natural and the biosynthetic IGF-I to be equipotent in every case except for a radioimmunoassay involving a monoclonal IGF-I antibody (the synthetic peptide had 2.4 times greater activity), and an IGF-II radioreceptor assay involving ovine placental membrane receptors (the natural peptide had 10-fold greater activity). We conclude that recombinant DNA-derived IGF-I is suitable for use, both as a standard and as a radioligand, in a wide variety of IGF assays.


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 Am. J. Clin. Nutr.Home page
J. C Brand-Miller, V. Liu, P. Petocz, and R. C Baxter
The glycemic index of foods influences postprandial insulin-like growth factor-binding protein responses in lean young subjects
Am. J. Clinical Nutrition, August 1, 2005; 82(2): 350 - 354.
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Copyright © 1987 by the American Association for Clinical Chemistry.