Characterization of a recombinant murine interleukin-6: assignment of disulfide bonds |
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Authors: | R J Simpson R L Moritz Van Snick" target="_blank">J Van RoostVan Snick |
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Institution: | Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Melbourne Branch, Australia. |
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Abstract: | 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. |
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