Oligosaccharide moieties

O Shannessy, D.J., and Quarles, R.H. (1985) Specific conjugation reactions of the oligosaccharide moieties of immunoglobulins./. Appl. Biochem. 7, 347-355. 

Glycoproteins are smaller than proteoglycans, and have far more variability in protein and carbohydrate content between different types. In both types of molecule, the oligosaccharide moieties are covalently attached to the protein via serine, threonine... 

In Figure 7, we present a stereo view of the superposition of the dominant conformers from the lowest energy two-state structural solutions, D A and D B and the one-state structural solutions B and C when all atoms in the oligosaccharide moiety of globoside were included in the comparison. In Figure 7, we also present... 

Takahashi N, Hitotsuya H, Hanzawa H, Arata Y, Kurihara Y, Structural study of asparagine-linked oligosaccharide moiety of taste-modifying protein, miraculin,... 

A comparison of direct O-mannosylation of serine or threonine on resin-bound peptides, with the incorporation of mannosylated serine or threonine building blocks, resulted in a higher overall yield for the building block approach (12.5 vs 5% for direct condensation). 134 Later it was demonstrated that resin-bound peptides are able to be glycosylated with different glycosyl trichloroacetimidates without protection of the hydroxy groups of the oligosaccharide moiety (Section 6.3.2.8). 135,136 ... 

Differences in the structure of glycoproteins can manifest themselves in a number of ways. Perhaps the first point to be emphasized is that the nature of the polypeptide chain to which oligosaccharide moieties become attached is not always the same. This is a situation that we have already discussed in connection with certain of the glycosaminoglycans (see p. 440). 

In all known types of CDG-I it has been observed that due to the loss of sialic acid residues, in addition to tetrasialo-transferrin, more or less pronounced di- and asialo-transferrin bands appear, which are evoked by the loss of either one or both complete oligosaccharide chains (Fig. 4.5.3, lanes 2-4). In contrast to CDG-I, changes in the charge of serum transferrin of most known CDG-II types are due to shortening of the oligosaccharide moieties (Fig. 4.5.3, lanes 5-7). 

Fig. 4.5.8 Examples for structures and molecular masses of 2-aminobenzamide (2-AB)-labelled oligosaccharide moieties derived from serum transferrin. Values below the oligosaccharide structures indicate the expected masses (in Da) by matrix-assisted laser desorption ionisation - time of flight analysis.

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