The separation of human insulin-like growth factors hIGF-1 and hIGF-2 was greatly improved by an additional purification step using the cation exchanger Mono-S (FPLC) compared to previous studies. Cross-reactions between hIFG-1 and hIGF-2 were strongly reduced. The more highly purified hIGF-1 had a cross-reaction of less than 1% in the RIA for hIGF-2, and was equivalent to recombinant hIGF-1. The pure hIGF-2 had a cross-reaction of less than 1% in the RIA for hIGF-1. In the human placental hIGF-2 radioreceptor assay, the hIGF-1 polypeptide competed less than 1% with hIGF-2 when the type 1 IGF receptor was blocked with insulin.
Rapid Communication| June 01 1988
An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process
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M. Tally, K. Florell, G. Enberg; An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process. Biosci Rep 1 June 1988; 8 (3): 293–297. doi: https://doi.org/10.1007/BF01115047
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