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Abstract
We investigated the influence of glycosylation on solubility, chromatographic behavior and resistance to heat- and chaotrope-dependent denaturation and proteolytic digestion of three recombinant human interferon gamma receptors produced in Escherichia coli, Spodoptera frugiperda and Chinese hamster ovary cells. The proteins produced in the eukaryotic expression systems were glycosylated, carrying different, heterogeneous carbohydrate moieties. They were assayed fully glycosylated and after removal of the oligosaccharides. Although glycosylation influenced the chromatographic behavior of the tested proteins, it did not protect against proteolysis and heat- or chaotrope-induced denaturation. The glycosylated receptors were slightly more sensitive to certain proteolytic cleavages and slightly less resistant to chaotropes, than the soluble receptor produced in Escherichia coli.
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