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An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process

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Abstract

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.

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Authors and Affiliations

  1. Department of Endocrinology, Karolinska Institutet, Box 60500, S-104 01, Stockholm, Sweden

    M. Tally, K. Florell & G. Enberg

Authors
  1. M. Tally
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  2. K. Florell
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  3. G. Enberg
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Tally, M., Florell, K. & Enberg, G. An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process. Biosci Rep 8, 293–297 (1988). https://doi.org/10.1007/BF01115047

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  • DOI: https://doi.org/10.1007/BF01115047

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