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. 2019 Jun 28;40(10):1364–1372. doi: 10.1038/s41401-019-0269-x

Fig. 3.

Fig. 3

K12C–E286C and S296C–S296C mutations significantly improved the heat resistance of AgUricase. The relative activity of wild-type (circle), K12C–E286C (square), and S296C–C302S (triangle) mutant AgUricase were measured after 30 min of incubation at various temperatures. The temperatures at which the enzymes retained half of their activity (Tm) were determined by fitting the curve to the equations (16) using GraphPad Prism 7 with R2 values > 0.99. The data are presented as the mean ± standard error of the means (SEM) of at least three independent experiments