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. 2016 Aug 19;6:31764. doi: 10.1038/srep31764

Figure 1. Purification of caspase-3 like activity from heat treated rice suspension cells.

Figure 1

(a) Caspase-3 active fractions from the G-75 column were pooled and purified further on a Mono-Q column equilibrated with 20 mM Tris/HCl buffer, pH 8.0. Proteins were eluted with a gradient of NaCl (0~1 M) in 20 mM Tris/HCl buffer, pH 8.0, at a flow rate of 1 ml/min. Proteins were detected by the absorbance at 280 nm. Peaks were collected respectively. (b) An equal amount of peaks collected from the Mono-Q column were incubated with Ac-DEVD-AMC. The AMC fluorescence was measured by a Microplate reader at 30 °C. RFU/h represented the differences of relative fluorescence units produced in 1h. I and II represent the peaks which exhibited caspase-3 like activity.