Glycoprotein glycosylation patterns

Although capable of glycosylating heterologous human proteins, the glycosylation pattern usually varies from the pattern observed on the native glycoprotein (when isolated from its natural source, or when expressed in recombinant animal cell culture systems). 

Post-translational modifications, in particular glycosylation patterns, can be incomplete and/or can differ very significantly from patterns associated with native human glycoproteins. 

The utilization of whole cells as bioreactors for the synthesis of oligosaccharides and engineering cell lines for the production of glycoproteins with a human-Hke glycosylation pattern are highlights in the field of glycobiotechnology. 

This procedure is not solely specific for carbohydrate side chains of proteins. Unglycosylated proteins may also be stained. To identify glycosylated proteins, the sample should be run in at least two identical lanes cut the gel and stain a lane with the common protein silver stain (Protocols 2.4.2.1 to 2.4.2.4) and the other lane by the described method. Compare pattern and intensity to identify glycoproteins. Glycosylated macromolecules are also stainable with Schiff s reagent (Protocol 2.4.4.1), but with less sensitivity. 

Several strategies have been developed to humanize the glycosylation patterns of proteins generated in transgenic plants. The first discussed here is the retention of glycoproteins within the ER. 

The most distinctive differences between the two glycoproteins are found in the glycosylation pattern of the N-terminal portion of the molecules, which forms the bulky dome. Here, variations of the chemical structure may have little or no morphological impact. 

As revealed in the preceding paragraphs, glycoproteins display a multitude of different glycosylation patterns. Owing to the biosynthetic pathways, the carbohydrate moieties of... 

With current technology, quantitative glycosylation analysis of therapeutic glycoproteins can be very challenging. The glycosylation patterns can be extremely complex with species that... 

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