The o-specific polysaccharide chain of campylobacter fetus serotype b lipopolysaccharide is a d-rhamnan terminated with 3-o -methyl-d-rhamnose (d-acofriose)
Senchenkova, Sof'ya N.
Shashkov, Alexander S.
Knirel, Yuriy A.
Mcgovern, Joseph J.
Moran, Anthony P.
MetadataShow full item record
This item's downloads: 0 (view details)
Cited 26 times in Scopus (view citations)
Senchenkova, Sof'ya N. Shashkov, Alexander S.; Knirel, Yuriy A.; Mcgovern, Joseph J.; Moran, Anthony P. (1996). The o-specific polysaccharide chain of campylobacter fetus serotype b lipopolysaccharide is a d-rhamnan terminated with 3-o -methyl-d-rhamnose (d-acofriose). European Journal of Biochemistry 239 (2), 434-438
An O-specific polysaccharide was liberated from Campylobacter fetus subsp. fetus serotype B lipopolysaccharide by mild acid hydrolysis followed by gel chromatography. This polysaccharide was found to contain D-rhamnose and 3-O-methyl-D-rhamnose (D-Rha3Me, D-acofriose) in a ratio of approximately 24:1, as well as lipopolysaccharide core constituents. The structure of the polysaccharide was studied by H-1-NMR and C-13-NMR spectroscopy, which included two-dimensional COSY, rotating-frame NOE spectroscopy (ROESY), and computer-assisted analysis of the C-13-NMR spectrum. Methylation analysis using [H-2(3)]methyl iodide and Smith degradation followed by GLC/MS of the derived acetylated oligosaccharide-alditols was used to determine the location of D-acofriose. The O-specific polysaccharide is linear, consists on average of 12 disaccharide repeating units, and is terminated by a residue of D-acofriose. The following structure of the D-rhamnan chain was established: [GRAPHICS] and fumarate as oxidant. Steady-state kinetics for the oxidase and the fumarate reductase activity of L-aspartate oxidase were obtained using either fumarate or oxygen as electron acceptor and L-aspartate as electron donor. Finally, succinate was identified as the product of the L-aspartate:fumarate oxidoreductase activity using radiolabeled fumarate under anaerobic conditions. The results suggest that fumarate can be a valuable alternative to oxygen as a substrate for L-aspartate oxidase.