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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...

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Main Authors: M., Sivapragasam, Abdullah, Norhafizah
Format: Article
Published: ESRSA Publications 2014
Online Access:http://psasir.upm.edu.my/id/eprint/35117/
http://www.ijert.org/view-pdf/8150/purification-of-glutathione-s-transferase-gst-using-mixed-mode-chromatography
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spelling my.upm.eprints.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
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
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.
format Article
author M., Sivapragasam
Abdullah, Norhafizah
spellingShingle M., Sivapragasam
Abdullah, Norhafizah
Purification of glutathione S-transferase (GST) using mixed mode chromatography
author_facet M., Sivapragasam
Abdullah, Norhafizah
author_sort M., Sivapragasam
title Purification of glutathione S-transferase (GST) using mixed mode chromatography
title_short 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_sort purification of glutathione s-transferase (gst) using mixed mode chromatography
publisher ESRSA Publications
publishDate 2014
url http://psasir.upm.edu.my/id/eprint/35117/
http://www.ijert.org/view-pdf/8150/purification-of-glutathione-s-transferase-gst-using-mixed-mode-chromatography
_version_ 1643831358037950464
score 13.209306

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