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- W1991417054 abstract "An inexpensive and fast-folding strategy for single-chain antibody (scFv) recovered from Escherichia coli inclusion bodies has been developed. Two anti-fluorescein single-chain antibodies, 4-4-20 and 4M5.3, were expressed as inclusion bodies in E. coli for use in a comparative refolding study. Active protein yields as well as degree of aggregation were evaluated for scFv produced by stepwise dialysis, redox dialysis, and a newly developed controlled dilution and filtration strategy. Although all three methods produced active protein for both 4-4-20 and 4M5.3, the extent of aggregation differed greatly among the methods. For 4-4-20, the controlled dilution and filtration strategy reduced aggregation by half, allowed batch processing times of 8h (an 18-fold improvement), and significantly reduced denaturant usage while increasing active yields by 150%. A hydroxyapatite resin polishing step was used to remove completely the aggregate species and inactive monomeric scFv from active scFv." @default.
- W1991417054 created "2016-06-24" @default.
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- W1991417054 date "2002-11-01" @default.
- W1991417054 modified "2023-09-25" @default.
- W1991417054 title "Rapid refolding and polishing of single-chain antibodies from Escherichia coli inclusion bodies" @default.
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- W1991417054 doi "https://doi.org/10.1016/s1046-5928(02)00538-7" @default.
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