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. 2013 Jan 2;161(3):1141–1157. doi: 10.1104/pp.112.206243

Figure 4.

Figure 4.

Biochemical characterization of the CaPIMT2 enzyme. A, Effect of temperature on the activity of purified recombinant CaPIMT2 enzyme. The specific activity was measured at different temperatures ranging from 0°C to 70°C. B, Effect of pH on the activity of purified recombinant CaPIMT2. The specific activity was measured at 37°C using different buffers (pH 3–6, citrate phosphate buffer; pH 6–8, sodium phosphate buffer; pH 8–10, 2-amino-2-methyl-1,3-propanediol buffer). C, Comparison of enzyme activity among CaPIMT1, CaPIMT2, ΔCaPIMT2 (CaPIMT2 lacking the 56-amino acid N terminus), and CaPIMT2′. Approximately 5 μg of purified protein was assayed in each case. Error bars in all graphs indicate se from three independent experiments.