Bio/Technology
9, 363 - 366 (1991)
doi:10.1038/nbt0491-363
Facilitated In Vitro Refolding of Human Recombinant Insulin-Like Growth Factor I Using a Solubilizing Fusion PartnerElisabet Samuelsson1, Henrik Wadensten2, Maris Hartmanis2, Tomas Moks1, *
& Mathias Uhlén1
1Department of Biochemistry and Biotechnology, Royal Institute of Technology, S-10044 Stockholm, Sweden.
2KabiGen AB, S-11287 Stockholm, Sweden.
*Corresponding author. 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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