Bisecting residue

Fig. 15.3 Plant and mammalian N-glycans have different structures. As illustrated here, a core structure (in gray) is common to plant and mammalian biantennary complex N-glycans. However, differences in the glycan processing machineries in plants and in mammals result in the absence of sialic acids in the terminal position of the antennae and the presence of a bisecting p (1,2) -xylose and of an a(l,3)-fucose residue in PMPs instead of the a(l,6)-fucose linked to the proximal N-acetylglucos-amine of native mammalian N-glycans.

C5-1 antibody was produced in alfalfa, the glycan component consisted predominantly of a mature oligosaccharide comprising a core a(l,3)-fucose residue, a bisecting P(l,2)-xylose residue and two terminal GlcNAc residues (Fig. 15.4) [6],... 

How close to the bifurcation limits does your bisection program succeed when the graphics solutions are used as starting points for fzero What are the sizes of the residues in the computed solutions near the bifurcation points Which of the proposed steady-state finders of part (a) or (b) do you prefer Be careful and monitor your hybrid algorithm s effort via clock and etime. 

Sasai K, Ikeda Y, Eguchi H, Tsuda T, Honke K, Taniguchi N. The achon of A-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalyhc step. FEBS Lett. 2002 522(1-3) 151-155. 

The molecular basis of inherited defects is established for a number of diseases and altered glycosylation patterns have been observed to be associated with these. For example, IgG Fc fragment conserved site glycans lacking in outer arm Gal residues increase in rheumatoid arthritis, tuberculosis and Crohn s disease. There is also an Fab-specific increase in glycans bearing a bisecting Gn and a core Fuc [148]. 

Bisected penta-antennary oligosaccharide found in hen ovomucoid. The GlcNAc-transferases (named with Roman numerals) are responsible for the addition of the GlcNAc residues that initiate antennae. The branches present in various multiantennary and bisected N-glycans are indicated. [Reproduced with permission from I. Brockhausen, Clinical aspects of glycoprotein biosynthesis. Crit. Rev. Clin. Lab. Sci. 30 68 (1993).]... 

Fig. I. Core structures of the carbohydrate units of nervous tissue glycoproteins. The structures are based on analytical data on rat brain glycoproteins and on assumptions of structural similarity with glycan cores from other sources. The main positions of variable or incomplete glycosylation are indicated by arrows. The approximate molar proportions of the glycans in rat brain and the mode of interaction with concanavalin A-Sepharose are indicated (the bisecting GicNAc residue affects the interaction of the diantennary glycans with concanavalin A) [9].

Gal(al-3)Gal group and 23% of the diantennary complex-type glycans contained the bisecting GlcNAc residue. These structures were not detected in the glycans of human plasma factor VIII. 

In contrast to sero- and lactotransferrins, glycans of ovotransferrins from avian egg-white contain a bisecting A-acetylglucosamine residue, like other glycoproteins from oviducts, such as ovomucoid and ovalbumin for instance (Fig. 16A-C). Like all of the avian egg glycoproteins, ovotransferrins are not fueosylated. 

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