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1.
FIG. 4.

FIG. 4. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Time course of GD3-FCHASE elongation. Purified MalE-NmC PST was incubated with the fluorescent acceptor GD3-FCHASE and analyzed by ion exchange HPLC as previously described (32).

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
2.
FIG. 6.

FIG. 6. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Competition of the PST elongation reaction with unlabeled acceptors. Trisialylated lactosyl-BODIPY (2.5 μM; dotted trace) was incubated with NmC PST (30 μg/ml) in the absence (black trace) or presence of 5 μM α-2,8-sialic acid trimer (maroon trace), α-2,8-hexamer (purple trace), or GD3 (blue trace).

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
3.
FIG. 5.

FIG. 5. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Comparison of acceptor activity of GD3 and sialic acid hexasaccharide. The ganglioside GD3 and a hexasaccharide isolated from the K92 polysaccharide were incubated as acceptors with purified MalE-NmC PST and CMP-[14C]sialic acid in an assay described in Materials and Methods. The hexasaccharide was prepared by digestion of K92 polysaccharides and purification by ion exchange and gel filtration as described previously (17, 32).

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
4.
FIG. 2.

FIG. 2. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Domain swap of NmB PST and NmC PST. Chimeras were constructed with nucleotides 1 to 439 of synD, 440 to 1479 of synE (pWV250), 1 to 322 of synD, and 323 to 1479 of synE (pWV245) as described in Materials and Methods. The chimeric enzymes were expressed and assayed, and the linkages of their polysialic acid products were determined by the sensitivity of the enzymatic reaction products to the α-2,8-NeuNAc-specific endoneuraminidase as described in Materials and Methods.

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
5.
FIG. 7.

FIG. 7. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

CMP-NeuNAc dependence of outer membrane acceptor elongation. A reaction mixture containing MalE-NmC PST, CMP-sialic acid, and OMV as described in Materials and Methods was applied to ELISA plates. The presence of meningococcal group C polysaccharide was detected with monoclonal antibodies to O-acetylated (closed triangles) and de-O-acetylated (closed circles) group C polysaccharides as described in Materials and Methods.

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
6.
FIG. 1.

FIG. 1. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Distribution of the MalE-NmC PST chimera, after PAGE of purified MalE-NmC PST. The ultracentrifugation pellet (lane 1), supernatant of a cell lysate of AD202(pWV243) (lane 2), and the major protein fractions eluted from the amylase column (lane 3) were loaded onto a 4-to-20% polyacrylamide SDS-PAGE gel. For Western blot analysis another gel was loaded with membrane fraction (lane A), the ultracentrifuge supernatant fraction of the BL21(pWV243) lysate (lane B), and the amylose-purified MalE-NmC PST (lane C). The gel was transferred to nitrocellulose, and the immunoblot was developed with anti-MalE antibody.

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.
7.
FIG. 3.

FIG. 3. From: Characterization and Acceptor Preference of a Soluble Meningococcal Group C Polysialyltransferase .

Native molecular size of the HaloTag-NmC PST chimera. A crude 25% saturation ammonium sulfate fraction of cell supernatant containing HaloTag-NmC polysialyltransferase was labeled as described in Materials and Methods. (A) The labeled lysate was applied to a Superose 12 FPLC column, and peak fractions were assayed for activity as described in Materials and Methods. (B) The labeled lysate (lane 4) was also applied to an SDS-PAGE gel, and labeled proteins (lanes 2 and 3) were detected under UV light.

Dwight C. Peterson, et al. J Bacteriol. 2011 April;193(7):1576-1582.

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