Abstract
The somatomedins insulin-like growth factors I and II (IGF-I and IGF-II) were originally isolated from human plasma by use of acid/ethanol extraction, gelfiltration and isoelectric focusing (IEF). With a semi-automated chromatography system we have similarily isolated IGF-I and II from human plasma. In this system the separation between IGF-I and II was achieved by ion-exchange chromatography and not with IEF. The crossreaction of native IGF-I in the radioimmunoassay (RIA) for IGF-II has generally been found to be about 10%. Biosynthetic IGF-I has, however, a crossreaction of only 1-2% in the RIA for IGF-II. The difference is most likely due to a contamination of IGF-II in the native IGF-I preparations.
By use of a Mono-S column (FPLC system) eluted with a salt gradient at pH 5.0, we have now achieved a complete separation between IGF-I and IGF-II. This finding might be of importance when interpreting results from earlier receptor studies with IGF-I and IGF-II.
Article PDF
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Enberg, G., Florell, K. & Hall, K. AN IMPROVED METHOD FOR THE PURIFICATION OF INSULIN-LIKE GROWTH FACTORS I AND II. Pediatr Res 20, 1191 (1986). https://doi.org/10.1203/00006450-198611000-00103
Issue Date:
DOI: https://doi.org/10.1203/00006450-198611000-00103