Recombinant human IL-6 expressed inE. coli undergoes selective N-terminal degradation: Evidence that the protein consists of a stable core and a nonessential flexible N-terminal
- 1 August 1993
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 12 (4), 489-497
- https://doi.org/10.1007/bf01025050
Abstract
A synthetic gene for human interleukin-6 has been expressed inE. coli. The protein has been purified and renatured and has the same activity as natural human IL-6 using the 7TD1 cell proliferation assay. The protein undergoes specific cleavage by a thiol protease, yielding two new N-termini at Arg-9 and His-15. The truncated proteins retain full biological activity. The degradation results in the loss of sharp amide resonances in the1H-NMR spectrum, and little change to the ultraviolet CD spectrum. Several amino acid type assignments could be made for these sharp amides using a DQF-COSY 2D-NMR experiment. The N-terminal 15 amino acids exist as a flexible, random coil, attached to a central structure.Keywords
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