The first EGF-like domain of human FVII (Figure 10.3) contains two serine residues that carry O-linked glycosylation [21,24,25]; both O-linked glycosylation sites are fully occupied in rFVIIa. For rFVIIa, three different glycan structures consisting of glucose, glucose-xylose, or glucose-(xylose)2 are found at S52 (Figure 10.4), while a single fucose is found at S60 (Figure 10.4).
The same O-linked carbohydrate structures are found in pdFVIIa with slightly different relative amounts of the three structures linked to S52 . In a study of the functional role of the O-linked glycosylation of FVIIa by use of site-specific mutants, it was suggested that the O-linked glycosylations could provide structural elements that were of importance for the association of FVIIa with the circulating TF pathway inhibitor .
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