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Purification of long helical capsid of Newcastle disease virus from Escherichia coli using anion exchange chromatography


Citation

Yap, Chee Fai and Tan, Wen Siang and Sieo, Chin Chin and Tey, Beng Ti (2013) Purification of long helical capsid of Newcastle disease virus from Escherichia coli using anion exchange chromatography. Biotechnology Progress, 29 (2). pp. 564-567. ISSN 8756-7938; ESSN: 1520-6033

Abstract

NPΔc375 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 NPΔc375 from clarified feedstock. This PB-AEC column adsorbed 76.2% of NPΔc375 from the clarified feedstock. About 67.5% of the adsorbed NPΔc375 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 NPΔc375 purified by SepFastTM Supor Q pre-packed column was as long as 490 nm and 22–24 nm in diameter. The antigenicity of the purified NPΔc375 was confirmed by enzyme-linked immunosorbent assay.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Institute of Bioscience
DOI Number: https://doi.org/10.1002/btpr.1697
Publisher: American Institute of Chemical Engineers
Keywords: Anion exchange chromatography; Long helical structure; Newcastle disease virus; Nucleocapsid protein; Escherichia coli
Depositing User: Nabilah Mustapa
Date Deposited: 21 Apr 2016 06:06
Last Modified: 21 Apr 2016 06:06
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1002/btpr.1697
URI: http://psasir.upm.edu.my/id/eprint/28069
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