Citation
Raksha, Sunhare and Tan, Wen Siang and Hamid, Muhajir and Ramanan, Ramakrishnan Nagasundara and Tey, Beng Ti
(2014)
A single-step purification of the glycoprotein of Nipah virus produced in insect cells using an anion exchange chromatography method.
Separation Science and Technology, 49 (2).
pp. 249-257.
ISSN 0149-6395; ESSN:1520-5754
Abstract
A single-step purification method based on an anion exchange chromatography was developed to purify truncated Nipah virus glycoprotein (tNiVG) expressed in Spodoptera frugiperda 9 (Sf9) insect cells. The preferred buffer conditions to bind and elute tNiVG protein were 50 mM sodium carbonate with pH 9 and 50 mM sodium citrate with pH 5, respectively. The use of elution buffer without sodium chloride separated the tNiVG protein from the tightly bound major host proteins and subsequently avoided the desalting step as one of the further downstream processes. About 90% purity and 89% recovery of tNiVG protein were achieved with the developed purification method.
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Additional Metadata
| Item Type: | Article |
|---|---|
| Divisions: | Faculty of Biotechnology and Biomolecular Sciences Institute of Bioscience |
| DOI Number: | https://doi.org/10.1080/01496395.2013.838265 |
| Publisher: | Taylor & Francis |
| Keywords: | Anion exchange chromatography; Enzyme-linked immunosorbent assay; Mass spectrometry; Spodoptera frugiperda 9; Truncated Nipah virus glycoprotein |
| Depositing User: | Nabilah Mustapa |
| Date Deposited: | 03 Jun 2015 12:16 |
| Last Modified: | 29 Oct 2015 08:02 |
| Altmetrics: | http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1080/01496395.2013.838265 |
| URI: | http://psasir.upm.edu.my/id/eprint/36282 |
| Statistic Details: | View Download Statistic |
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