Characterization of a recombinant murine interleukin-6: assignment of disulfide bonds.
Murine interleukin 6 (mIL-6) has been synthesized as a fusion protein using a lac operon inducible plasmid in Escherichia coli. The first 8 amino acids are from the N-terminus of bacterial beta-galactosidase and the last 175 amino acids are from residue number 12 to the end of native mIL-6. This fusion protein is equipotent with the native molecule in the hybridoma growth factor assay and has comparable receptor binding characteristics. The two disulfide bridges in mIL-6 have been identified by Staphylococcus aureus V8 protease peptide mapping and Edman degradation of cystine-containing peptides. It has been shown that there are disulfide bonds between Cys46-Cys52 and Cys75-Cys85.
Simpson
R J
RJ
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Melbourne Branch, Australia.
Moritz
R L
RL
Van Roost
Van Snick
J
J
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides; D015850:Interleukin-6; D007378:Interleukins; D051379:Mice; D010084:Oxidation-Reduction; D010449:Peptide Mapping; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins
D004220:Disulfides; D015850:Interleukin-6; D007378:Interleukins; D011993:Recombinant Fusion Proteins