ISSN:
1573-4943
Keywords:
Interleukin-6
;
recombinant DNA technology
;
proteolytic degradation
;
NMR
;
N-terminal flexibility
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01025050
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