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Recombinant human interferon alpha-2b was renatured using guanidine hydrochloride(cas 50-01-1) concentration gradient exclusion chromatography (SEC)

Recombinant human interferon alpha-2b was renatured using guanidine hydrochloride(cas 50-01-1) concentration gradient exclusion chromatography (SEC) method. The effects of the concentration of guanidine hydrochloride on the concentration of guanidine hydrochloride, the gradient length, the flow rate and the ratio of reduced / oxidized glutathione (GSH /GSSG) in the refolding solution were investigated. 
The results showed that the recovery rate of rhIFNα-2b protein was 1.5 times of that of dialysis refolding method, the activity of protein was 68.7%, the specific activity was 1.77 × 10 ~ 8IU /mg, and the purity was 94%. The recombinant human interferon α-2b was efficiently renatured with the guanidine hydrochloride(cas 50-01-1) concentration gradient ion exchange chromatography (IEC) as a protein renaturation system, and the protein was purified at the same time. The specific activity of recombinant human interferon α-2b was 1.13 × 10 ~ 8IU /mg after refolding under the conditions of flow rate of 0.5ml /min, guanidine hydrochloride concentration of 1.5mol /L and sample loading of 2.24mg. The recovery was 51.2%, the protein activity was 46.3% and the purity was higher than 90%. Recombinant human interferon alpha - 2b by hydrophobic chromatography(HIC) method. When the flow rate is 1ml /min, the concentration of guanidine hydrochloride is 2mol /L in Buffer A and Buffer B, the specific activity of rhIFNα-2b is 2.34 × 10 ~ 8IU / mg after refolding, and the protein recovery 37.2%, the protein activity was 57.2% and the purity was up to 92%.

 

 

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