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- W2079666119 abstract "Glycosylation of proteins fulfills important functions and because of its diversity contributes to apparent protein heterogeneity. We investigated the heterogeneity of a fusion protein comprising the extracellular domain of the human interferon-γ (IFN-γ) receptor and parts of the human IgG3 constant region, a potential IFN-γ antagonist. The protein was produced in Chinese hamster ovary (CHO) cells and was secreted into the culture medium as an 175 kD glycoprotein. Glycosylation represented approximately one-third of the apparent molecular mass of the fusion protein, consisted of N- and O-linked carbohydrate moieties, and included sialic acid residues as part of both N- and O-linked oligosaccharides. Fusion protein forms with different apparent molecular masses and charges were separated by ion-exchange chromatography. Preparative electrofocusing revealed a wide spectrum of glycoforms. Glycosylation of the fusion protein and of soluble IFN-γ receptors, comprising the extracellular domain of the native sequence, expressed in insect and CHO cells did not interfere with affinity of ligand binding." @default.
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- W2079666119 date "1995-04-01" @default.
- W2079666119 modified "2023-10-17" @default.
- W2079666119 title "Interferon-γ Receptor Extracellular Domain—IgG Fusion Protein Produced in Chinese Hamster Ovary Cells as Mixture of Glycoforms" @default.
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- W2079666119 doi "https://doi.org/10.1089/jir.1995.15.309" @default.
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