Abstract
We describe a new approach to refolding recombinant proteins in which an affinity fusion partner, consisting of two IgG-binding domains (ZZ) derived from sta-phylococcal protein A, is used to solubi-lize misfolded molecules before, during and after reduction and reoxidation. We show that human insulin-like growth factor I (IGF-I) can be refolded as a fusion protein at a concentration as high as 1–2 mg/ml without the use of denaturing agents. A process scheme suitable for large scale application is described in which the yield of correctly folded human IGF-I with full biological activity is substantially increased.
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Samuelsson, E., Wadensten, H., Hartmanis, M. et al. Facilitated In Vitro Refolding of Human Recombinant Insulin-Like Growth Factor I Using a Solubilizing Fusion Partner. Nat Biotechnol 9, 363–366 (1991). https://doi.org/10.1038/nbt0491-363
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DOI: https://doi.org/10.1038/nbt0491-363
