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. 2006 Mar 15;395(Pt 1):211–221. doi: 10.1042/BJ20051657

Figure 3. FPLC gel-filtration chromatography on Superose 12HR column of the sPPase purified from whole cells and cyanelles of Cy. paradoxa.

Figure 3

Aliquots (0.1 ml) of sPPase preparations (hydroxyapatite eluate) purified from whole cells (approx. 150 μg) (A) or isolated cyanelles (approx. 50 μg) (B) were applied on to a Superose 12HR 10/30 column. Elution (0.4 ml/min) and fractions were collected as described in Figure 2. The upper inset shows the calibration of the column with protein standards (FER, ferritine; CAT, catalase; ALD, aldolase; LPD, lipoamide dehydrogenase; OVA, ovoalbumin; CYT, cytochrome c) and the position of sPPase peaks (triangle and grey circle) that corresponds to a native molecular mass of approx. 33 kDa. The Coomassie-Blue-stained SDS/PAGE gels of the indicated fractions around the activity peak (*, highest activity fraction) show a single 32 kDa protein (arrows) that co-eluted with sPPase activity in both cases. The positions and molecular masses of protein standards are indicated on the left-hand side of the SDS/PAGE gels.