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Based on affinity principles, methods were developed to facilitate
in vivo folding (1,3,4). The principle, applied on human Insulin-like
Growth factor type 1 (IGF-I), was based on the co-expression
of a binding molecule with affinity to the correct folding
form. Affinity principles was also used to develop novel purification
methods (2) based on Exbanded Bed Adsoption (EBA). Recombinant
proteins could be recovered directly from the culture medium
of E.coli based on a secretion system developed earlier (5).
| Key publications: |
| 1. |
Samuelsson, Wadensten, Hartmanis,
Moks & Uhlen Facilitated in vitro refolding of human
recombinant insulin-like growth factor I using a solubilizing
fusion partner. Nature Biotechnol 9, 363-366 (1991). |
| 2. |
Hansson, Stahl, Hjorth, Uhlen & Moks
Single-step recovery of a secreted recombinant protein by
expanded bed adsorption. Nature Biotechnol 12, 285-288 (1994). |
| 3. |
Samuelsson, Jonasson, Viklund, Nilsson &
Uhlen Affinity-assisted in vivo folding of a secreted human
peptide hormone in Escherichia coli. Nat Biotechnol 14,
751-755 (1996). |
| 4. |
Samuelsson & Uhlen Chaperone-like effect
during in vitro refolding of insulin-like growth factor
I using a solubilizing fusion partner. Ann N Y Acad Sci
782, 486-494 (1996). |
5. |
Abrahmsen, Moks, Nilsson & Uhlen Secretion
of heterologous gene products to the culture medium of Escherichia
coli. Nucleic Acids Res 14, 7487-7500 (1986) |
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