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      Phosphorylation of glutathione-S-transferase by protein kinase C-alpha implications for affinity-tag purification.

      Biotechnology Letters
      Animals, Chromatography, Affinity, Electrophoresis, Gel, Two-Dimensional, Glutathione Transferase, genetics, metabolism, Phosphorylation, Protein Kinase C-alpha, Recombinant Fusion Proteins, isolation & purification, Schistosoma japonicum, enzymology, Serine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

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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 2,500 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-alpha (PKC-alpha) 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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