Abstract
A recombinant human consensus interferon-α mutant (cIFN) was expressed in Pichia pastoris. The maximum dry cell weight, cIFN concentration and antiviral activity were 160 g l−1, 1.24 g l−1 and 4.1 × 107 IU ml−1, respec tively. The cIFN secreted into the medium was in the form of aggregates dominantly by non-covalent interaction and partially by disulphide bond. When the fermentation supernatant was disaggregated with 6 M guanidine hydrochloride, the antiviral activity of cIFN achieved 2.2 × 108 IU ml−1.
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Acknowledgments
We thank Dr. Zhimin Liu for Pichia pastoris GS115/pPIC9-cIFN cells and Mr. Kanghua Wu for his help in fermentation and Mrs. Qiqi Shi for electrophoresis analysis. This work was supported by the National High Technology Research and Development Program of China (863 Program, No. 2002aa217021; 2002aa2z3451).
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Hao, Y., Chu, J., Wang, Y. et al. Expression and Aggregation of Recombinant Human Consensus Interferon-α Mutant by Pichia pastoris . Biotechnol Lett 28, 905–909 (2006). https://doi.org/10.1007/s10529-006-9024-8
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DOI: https://doi.org/10.1007/s10529-006-9024-8