Journal: Journal of Proteome Research
Article Title: Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL
doi: 10.1021/pr300806b
Figure Lengend Snippet: Post-transfer processing of N-glycans in the Dictyostelium HL241 strain. A proposed scheme for the modification of N-glycans in the HL241 strain commencing after the transfer of Man 6 GlcNAc 2 (boxed). Whereas the anionic modifications and the intersecting N- acetylglucosamine residue can be found on both Man 5 GlcNAc 2 and Man 6 GlcNAc 2 scaffolds, the transfer of fucose and bisecting N- acetylglucosamine appears to be dependent on the prior removal of one terminal α1,2-mannose residue from the A branch. Reactions for which there is evidence from the literature are shown with solid arrows ; for some reactions involving fucosylated glycans, the order of processing is unclear and so these are indicated with dashed arrows . The predicted antibody or lectin reactivity status (anti-Man6P, anti-HRP or WGA) of the four glycans at the foot of the diagram is also indicated.
Article Snippet: After blocking with 0.5% (w/v) bovine serum albumin in Tris-buffered saline, the membranes were incubated with rabbit antihorseradish peroxidase (anti-HRP, Sigma-Aldrich; 1:10 000) or biotin-conjugated wheat germ agglutinin lectin (WGA, Vector Laboratories; 1:2000).
Techniques: Modification