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• W2045493621 abstract "NP Δc375 is a truncated version of the nucleocapsid protein of Newcastle disease virus (NDV) which self‐assembles into a long helical structure. A packed bed anion exchange chromatography (PB‐AEC), SepFastTM Supor Q pre‐packed column, was used to purify NP Δc375 from clarified feedstock. This PB‐AEC column adsorbed 76.2% of NP Δc375 from the clarified feedstock. About 67.5% of the adsorbed NP Δc375 was successfully eluted from the column by applying 50 mM Tris‐HCl elution buffer supplemented with 0.5 M NaCl at pH 7. Thus, a recovery yield of 51.4% with a purity of 76.7% which corresponds to a purification factor of 6.5 was achieved in this PB‐AEC operation. Electron microscopic analysis revealed that the helical structure of the NP Δc375 purified by SepFast TM Supor Q pre‐packed column was as long as 490 nm and 22–24 nm in diameter. The antigenicity of the purified NP Δc375 was confirmed by enzyme‐linked immunosorbent assay. © 2013 American Institute of Chemical Engineers Biotechnol. Prog ., 29: 564–567, 2013" @default.
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• W2045493621 date "2013-03-01" @default.
• W2045493621 modified "2023-10-18" @default.
• W2045493621 title "Purification of long helical capsid of newcastle disease virus from<i>Escherichia coli</i>using anion exchange chromatography" @default.
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• W2045493621 doi "https://doi.org/10.1002/btpr.1697" @default.
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