Effect of Protein Primary Sequence on N-Glycosylation of Recombinant Human Soluble Thy-1
2014
Devasahayam, Mercy
The primary sequence of a proteinis assumed to have an effect on N-glycosylation. This was studied by comparing the N-glycosylation profiles of rat and human soluble Thy-1 an IgSF glycoprotein molecule. The oligosaccharide profile of human sThy-1 which share 66% amino acid identity with rat Thy-1 from CHO-K1 cells was compared. The distribution of neutral and charged oligosaccharides across species was shown to be similar. However, in recombinant human sThy-1 as already seen in native human Thy-1 hybrid oligosaccharides were present which are not present in recombinant or native rat Thy-1. This indicates that the protein primary structure plays a primary role in N-glycosylation. The article demonstrates that cell type specifies glycoform heterogeneity of the attached oligosaccharides but not N-glycosylation sequon occupancy. While the position of the N-glycosylation sequon in the protein primary sequence determines accessibility to the oligosaccharide modifying enzymes leading to site specific glycosylation.
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