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Interferon was extracted by guanidine hydrochloride(50-01-1)

To investigate the isolation and purification of recombinant human interferon α2a without monoclonal antibody affinity chromatography.
Interferon was extracted with 7 mmol L-1 guanidine hydrochloride(50-01-1) and then treated with metal chelate chromatography, ion exchange chromatography, chromatography and gel filtration were used to purify the extracted interferon.
The target protein was purified by 195.1 times and the specific activity of the protein was 2.40 × 108 IU @ mg-1, and the recovery rate was 30.1%. SDS-PAGE was a band Quality is about 19 kD, purity is greater than 97%.
The process reduces the production cost, easy to expand the scale of production, suitable for industrial requirements.

 

 

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