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- W2012383552 abstract "We have characterized the heterogeneity of recombinant human interferon-γ (IFN-γ) produced by three expression systems: Chinese hamster ovary cells, the mammary gland of transgenic mice, and baculovirus-infected Spodoptera frugiperda (Sf9) insect cells. Analyses of whole IFN-γ proteins by electrospray ionization-mass spectrometry (ESI-MS) from each recombinant source revealed heterogeneous populations of IFN-γ molecules resulting from variations in N-glycosylation and C-terminal polypeptide cleavages. A series of more specific analyses assisted interpretation of maximum entropy deconvoluted ESI-mass spectra of whole IFN-γ proteins; MALDI-MS analyses of released, desialylated N-glycans and of deglycosylated IFN-γ polypeptides were combined with analyses of 2-aminobenzamide labeled sialylated N-glycans by cation-exchange high-performance liquid chromatography. These analyses enabled identification of specific polypeptide cleavage sites and characterization of associated N-glycans. Production of recombinant IFN-γ in the mammalian expression systems yielded polypeptides C-terminally truncated at dibasic amino acid sites. Mammalian cell derived IFN-γ molecules displayed oligosaccharides with monosaccharide compositions equivalent to complex, sialylated, or high-mannose type N-glycans. In contrast, IFN-γ derived from baculovirus-infected Sf9 insect cells was truncated further toward the C-terminus and was associated with neutral (nonsialylated) N-glycans. These data demonstrate the profound influence of host cell type on posttranslational processing of recombinant proteins produced in eukaryotic systems." @default.
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- W2012383552 date "1996-02-01" @default.
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- W2012383552 title "Posttranslational processing of recombinant human interferon-γ in animal expression systems" @default.
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- W2012383552 doi "https://doi.org/10.1002/pro.5560050217" @default.
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