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• W2019946756 abstract "Two mixed-mode resins were evaluated as an alternative to conventional affinity resins for the purification of recombinant proteins fused to maltose-binding protein (MPB). We purified recombinant MBP, MBP-LacZ and MBP-Leap2 from crude Escherichia coli extracts. Mixed-mode resins allowed the efficient purification of MBP-fused proteins. Indeed, the quantity of purified proteins was significantly higher with mixed-mode resins, and their purity was equivalent to that obtained with affinity resins. By using purified MBP, MBP-LacZ and MBP-Leap2, the dynamic binding capacity of mixed-mode resins was 5-fold higher than that of affinity resins. Moreover, the recovery for the three proteins studied was in the 50–60% range for affinity resins, and in the 80–85% range for mixed-mode resins. Mixed-mode resins thus represent a powerful alternative to the classical amylose or dextrin resins for the purification of recombinant proteins fused to maltose-binding protein." @default.
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• W2019946756 date "2009-05-01" @default.
• W2019946756 modified "2023-09-27" @default.
• W2019946756 title "Efficient purification of recombinant proteins fused to maltose-binding protein by mixed-mode chromatography" @default.
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• W2019946756 doi "https://doi.org/10.1016/j.chroma.2009.03.048" @default.
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