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The preassembled sugar chain allows better quality control. The assembled oligosaccharide chains can be checked for accuracy before they are added to the protein; if a mistake were made in adding sugars individually to the protein, the whole protein would have to be discarded. Because far more energy is used in building a protein than in building a short oligosaccharide chain, this is a much more economical strategy. This difficulty becomes apparent as the protein moves to the cell surface: although sugar chains are continually modified by enzymes in various compartments of the secretory pathway, these modifications are often incomplete and result in considerable heterogeneity of the glycoproteins that leave the cell. This heterogeneity is largely due to the restricted access that the enzymes have to the sugar trees attached to the surface of proteins. The heterogeneity also explains why glycoproteins are more difficult to study and purify than nonglycosylated proteins.

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Q: Why might it be advantageous to add a preassembled block of 14 sugar residues to a protein in the ER rather than building the sugar chains step-by-step on the surface of the protein by the sequential?
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