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- W2993122051 abstract "[Objective] To study the purification of recombinant porcine interferon-alpha(rPoIFN-alpha) and lay a foundation for researches on the structure of the rPoIFN-alpha and the preparation of standard proteins.[Method] The rPoIFN-alpha were induced and extracted from the recombinant E.coli BL21,and they were purified by two strategies.The first strategy was that the rPoIFN-alpha were purified by GST(glutathione S transferase) affinity chromatography,DEAE(diethylaminoethyl) anion exchange chromatography and gel filtration in turn defined as three-step chromatography method;the second strategy was that the rPoIFN-alpha were purified by GST affinity chromatography and gel filtration in turn defined as two-step chromatography method.Then the purified products were detected by the SDS-PAGE(sodium dodecyl sulfate polyacrylamide gel electrophoresis) and were identified by western-blotting.[Result] The purity quotient of purified products of the two-step chromatography method was 96.0% and that of the three-step chromatography method was 98.8%.The purified products were detected by the SDS-PAGE and the western-blotting,respectively.The results showed that the target band was 45.0 kDa and the specific band was found.[Conclusion] The purity quotient of proteins of the two-step chromatography method is close to that of the three-step chromatography method,thus the two-step chromatography method is more convenient and more suitable for pilot production than the three-step chromatography method." @default.
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- W2993122051 date "2010-01-01" @default.
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- W2993122051 title "Purification of recombinant porcine interferon-alpha." @default.
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