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. 2010 Mar 1;78(5):1832–1840. doi: 10.1128/IAI.00446-09

FIG. 1.

FIG. 1.

Analysis of PDE activity of CdpA in vitro. PDE activity of CdpA was assessed in vitro using 1 μM, 2.5 μM, and 5.0 μM purified MBP-CdpA protein or MBP and 5 mM bis-pNPP substrate. The chart showed a dose-dependent catalysis of the release of p-nitrophenol by increasing concentration of recombinant MBP-CdpA protein. Absorbance at 410 nm was read against an enzyme blank without any protein. Black bars represent p-nitrophenol release catalyzed the recombinant MBP-CdpA protein and white bars represent the contaminating PDE activity from E. coli purified MBP protein.