Citation
M., Sivapragasam and Abdullah, Norhafizah
(2014)
Purification of glutathione S-transferase (GST) using mixed mode chromatography.
International Journal of Engineering Research & Technology, 3 (2).
pp. 1292-1299.
ISSN 2278-0181
Abstract
A simple and small scale laboratory method to compare between ultrasonication, glass bead shaking and chemical lysis were evaluated for the release of recombinant Glutathione S-Transferase (GST) from Escherichia coli. Since the protein Glutathione S-Transferase is expressed intracellularly, cell disruption process is the precursor step for protein recovery.GST was purified using assessment with PPA and HEA HyperCel resin. Optimum release of GST was via ultrasonication, 70% amplitude size with enzyme release of 129.9 U/mL. Purification yields via PPA HyperCel yielded 96% recovery while purification using HEA HyperCel yielded a 93% enzyme recovery.
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Additional Metadata
| Item Type: | Article |
|---|---|
| Divisions: | Faculty of Engineering |
| Publisher: | ESRSA Publications |
| Keywords: | Glutathione S-transferase; Chromatography; Intracellular protein; PPA HyperCel; HEA HyperCel |
| Depositing User: | Nurul Ainie Mokhtar |
| Date Deposited: | 30 Dec 2015 10:58 |
| Last Modified: | 30 Dec 2015 10:58 |
| URI: | http://psasir.upm.edu.my/id/eprint/35117 |
| Statistic Details: | View Download Statistic |
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