Purification of glutathione S-transferase (GST) using mixed mode chromatography
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 dis...
| Main Authors: | , |
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| Format: | Article |
| Published: |
ESRSA Publications
2014
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| Online Access: | http://psasir.upm.edu.my/id/eprint/35117/ |
| _version_ | 1848847964743663616 |
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| author | M., Sivapragasam Abdullah, Norhafizah |
| author_facet | M., Sivapragasam Abdullah, Norhafizah |
| author_sort | M., Sivapragasam |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T09:26:58Z |
| format | Article |
| id | upm-35117 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T09:26:58Z |
| publishDate | 2014 |
| publisher | ESRSA Publications |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-351172015-12-30T10:58:20Z http://psasir.upm.edu.my/id/eprint/35117/ Purification of glutathione S-transferase (GST) using mixed mode chromatography M., Sivapragasam Abdullah, Norhafizah 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. ESRSA Publications 2014-02 Article PeerReviewed 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 http://www.ijert.org/view-pdf/8150/purification-of-glutathione-s-transferase-gst-using-mixed-mode-chromatography |
| spellingShingle | M., Sivapragasam Abdullah, Norhafizah Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title | Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title_full | Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title_fullStr | Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title_full_unstemmed | Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title_short | Purification of glutathione S-transferase (GST) using mixed mode chromatography |
| title_sort | purification of glutathione s-transferase (gst) using mixed mode chromatography |
| url | http://psasir.upm.edu.my/id/eprint/35117/ http://psasir.upm.edu.my/id/eprint/35117/ |