Recombinant human IL-6 expressed in E. coli undergoes selective N-terminal degradation: evidence that the protein consists of a stable core and a nonessential flexible N-terminal
| Autor: | Steven C. Brown, Eric H. Kawashima, Jean-Yves Bonnefoy, Amanda E. I. Proudfoot, Alain R. Bernard |
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| Rok vydání: | 1993 |
| Předmět: |
Circular dichroism
Magnetic Resonance Spectroscopy Stereochemistry Molecular Sequence Data Biology Cleavage (embryo) medicine.disease_cause Biochemistry law.invention law medicine Escherichia coli Genes Synthetic Humans Amino Acid Sequence Peptide sequence chemistry.chemical_classification Base Sequence Interleukin-6 Circular Dichroism Biological activity Random coil Recombinant Proteins Amino acid chemistry Recombinant DNA |
| Zdroj: | Journal of protein chemistry. 12(4) |
| ISSN: | 0277-8033 |
| Popis: | A synthetic gene for human interleukin-6 has been expressed in E. 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 the 1H-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. |
| Databáze: | OpenAIRE |
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