A strategy for purifying glutathione S-transferase in the presence of sodium dodecyl sulfate

Glutathione S-transferase (GST) is widely used to prepare and purify GSTtagged fusion proteins. Although GST improves protein solubility, detergents must often be used to achieve protein solubilization from bacterial lysates. However, purification of GST by affinity chromatography cannot be achieved...

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Détails bibliographiques
Publié dans:BioTechniques. - 1991. - 51(2011), 3 vom: 01. Sept., Seite 193-4
Auteur principal: Boisselier, Elodie (Auteur)
Autres auteurs: Audet, Marie Lou, Cantin, Line, Salesse, Christian
Format: Article en ligne
Langue:English
Publié: 2011
Accès à la collection:BioTechniques
Sujets:Journal Article Research Support, Non-U.S. Gov't Glycols Recombinant Fusion Proteins Sodium Dodecyl Sulfate 368GB5141J Glutathione Transferase EC 2.5.1.18 hexylene glycol KEH0A3F75J
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245 1 2 |a A strategy for purifying glutathione S-transferase in the presence of sodium dodecyl sulfate 
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520 |a Glutathione S-transferase (GST) is widely used to prepare and purify GSTtagged fusion proteins. Although GST improves protein solubility, detergents must often be used to achieve protein solubilization from bacterial lysates. However, purification of GST by affinity chromatography cannot be achieved in the presence of even low concentrations of the detergent sodium dodecyl sulfate (SDS). Here we show that 2-methyl-2,4-pentanediol (MPD) can prevent SDS from interfering with purification of GST, thus enabling purification of proteins that require SDS to improve their solubility 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Recombinant Fusion Proteins  |2 NLM 
650 7 |a Sodium Dodecyl Sulfate  |2 NLM 
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700 1 |a Cantin, Line  |e verfasserin  |4 aut 
700 1 |a Salesse, Christian  |e verfasserin  |4 aut 
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