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. 2009 Jul 31;66(18):3081–3090. doi: 10.1007/s00018-009-0101-8

Fig. 3.

Fig. 3

Autophosphorylation levels and kinase activities of GST-Pfnek3 alanine-substituted mutants. a Purified wild-type GST-Pfnek3 and the indicated mutants were resolved by SDS-PAGE and stained with the phosphoprotein gel stain to assess their autophosphorylation levels. In the protein standard marker (M), the 70-kDa protein band corresponds to a phosphoprotein that could be detected using the phosphostain. Following phosphostaining, the gel was stained with Coomassie Blue to ensure that relatively equal amounts of proteins were loaded. b The in vitro kinase activities of the respective GST-Pfnek3 mutants were subsequently determined by their ability to phosphorylate the MBP substrates. ND Kinase activity not detected