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Effect of Glycosylation on Properties of Soluble Interferon Gamma Receptors Produced in Prokaryotic and Eukaryotic Experession Systems

Bio/Technology volume 10, pages 1143–1147 (1992)Cite this article

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 γ 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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Author notes

  1. Michael Fountoulakis: Corresponding author at: F. Hoffmann-La Roche Ltd., PRTB, Bldg. 15-16, CH-4002 Basel, Switzerland.

Authors and Affiliations

  1. F. Hoffmann-La Roche Ltd., Pharmaceutical Research-New Technologies, CH-4002, Basel, Switzerland

    Michael Fountoulakis & Reiner Gentz

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  1. Michael Fountoulakis
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  2. Reiner Gentz
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Fountoulakis, M., Gentz, R. Effect of Glycosylation on Properties of Soluble Interferon Gamma Receptors Produced in Prokaryotic and Eukaryotic Experession Systems. Nat Biotechnol 10, 1143–1147 (1992). https://doi.org/10.1038/nbt1092-1143

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  • DOI: https://doi.org/10.1038/nbt1092-1143

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