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. Author manuscript; available in PMC: 2009 Dec 12.
Published in final edited form as: Biochem Biophys Res Commun. 2008 Oct 23;377(2):710–713. doi: 10.1016/j.bbrc.2008.10.062

Figure 1. Effects of mutations of the KKVEW sequence of Inh3 on the inhibition of PP1 activity.

Figure 1

The V41D, E42C, W43A mutants of Inh3 were purified to near-homogeneity and their abilities to inhibit PP1 activity were determined as a function of concentration (Experimental Procedures). Results were plotted as percentage of inhibition of phosphorylase phosphatase activity: wild type Inh3, circles; Inh3-E42C, squares; Inh3-W43A, triangles; Inh3-V41D, inverted triangles.