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Phosphorylation of Glutathione-S-transferase by Protein Kinase C-α Implications for Affinity-Tag Purification

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Abstract

Expression and purification of proteins as fusions with glutathione S-transferase (GST) is a standard and widely employed system. In more than 2500 published studies, GST has been used to facilitate the purification of recombinant proteins, assess protein–protein interactions, and establish protein function. In this report, we provide evidence that GST can be phosphorylated in vitro by protein kinase C-α (PKC-α) at Ser-93. Therefore, since GST itself may be a target for a number of catalytic enzymes, failure to remove the GST tag from the recombinant protein may lead to inaccurate conclusions.

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Correspondence to Patricia Rodriguez.

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Rodriguez, P., Mitton, B. & Kranias, E.G. Phosphorylation of Glutathione-S-transferase by Protein Kinase C-α Implications for Affinity-Tag Purification. Biotechnol Lett 27, 1869–1873 (2005). https://doi.org/10.1007/s10529-005-3895-y

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  • DOI: https://doi.org/10.1007/s10529-005-3895-y

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