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. Author manuscript; available in PMC: 2013 Nov 21.
Published in final edited form as: Biochem Biophys Res Commun. 2009 Jan 23;380(3):10.1016/j.bbrc.2009.01.108. doi: 10.1016/j.bbrc.2009.01.108

Figure 3. Activity of P. aeruginosa neuraminidase mutations.

Figure 3

Site-directed mutations were made within the active site of P. aeruginosa neuraminidase or truncation in the C-terminus (deleting residues 334-438) and purified protein used to determine neuraminidase activity compared to wild-type enzyme (WT, control) using the fluorogenic substrate 2’-(4-methylumbelliferyl)-α-D-N-acetylneuraminic acid. *p-value <0.05.