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. 2007 Aug 17;104(35):13930–13935. doi: 10.1073/pnas.0704915104

Fig. 3.

Fig. 3.

Characterization of the interaction between ZPR1 and eEF1A. (A) Quantitative analysis of the binding of ZPR1 constructs to eEF1A loaded with mant–GDP or mant–guanyl-5′yl-imidodiphosphate. Solid lines represent fitted model functions for a hyperbolic binding isotherm. (B) Coprecipitation of eEF1A or the preformed eEF1A–eEF1Bα116–206 complex with GST–ZPR11–240. Note that eEF1A and GST-ZPR11–240 have identical mobility on SDS/PAGE. (C) Coprecipitation of eEF1A or the preformed eEF1A–His6 ZPR11–240 complex with GST–eEF1Bα116–206.