Title : High yield refolding and purification process for recombinant human interleukin-6 expressed in Escherichia coli.

Pub. Date : 1999 Feb 5

PMID : 10099541






2 Functional Relationships(s)
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1 Quantitative reconstitution of the native disulfide bonds of hIL-6 from the fully denatured E. coli extracts could be performed by glutathione-assisted oxidation in a completely denaturating condition (6M guanidinium chloride) at protein concentrations higher than 1 mg/mL, preventing aggregation of reduced hIL-6. Glutathione interleukin 6 Homo sapiens
2 Quantitative reconstitution of the native disulfide bonds of hIL-6 from the fully denatured E. coli extracts could be performed by glutathione-assisted oxidation in a completely denaturating condition (6M guanidinium chloride) at protein concentrations higher than 1 mg/mL, preventing aggregation of reduced hIL-6. Glutathione interleukin 6 Homo sapiens