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Fig. 4 | Gut Pathogens

Fig. 4

From: Validating the inhibitory effects of d- and l-serine on the enzyme activity of d-3-phosphoglycerate dehydrogenases that are purified from Pseudomonas aeruginosa, Escherichia coli and human colon

Fig. 4

The optimum ionic strength of the purified PGDHs derived from three different species. The optimal activity (mU/mg) of each PGDH was determined by performing the PGDH activity assay in the reaction mixture containing various concentrations of Tris–HCl buffer. The assay was performed in triplicate, and data being shown as the mean activity (mU/mg) ± SD. a A significant difference was observed in the P. aeruginosa PGDH activity measured at 50 mM versus at 200 mM and 10 mM (*P < 0.05), but not between P. aeruginosa PGDH activity at 50 mM versus at 100 mM (ns: not significant, P > 0.05). b A significant difference was observed between E. coli PGDH activity at 100 mM and that at 50 mM and 10 mM (*P < 0.05), but not between E. coli PGDH activity at 100 mM and that at 200 mM (ns). c A significant difference was observed between human PGDH activity at 200 mM and that at 50 mM and 10 mM (*P < 0.05), but not between human PGDH activity at 200 mM and that at 100 mM (ns)

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