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- W1233964385 abstract "Publisher Summary This chapter describes procedures used for expressing human interferon (IFN)-β in CHO cells, modifying the gene sequence encoding the carbohydrate attachment site of IFN-β, and analyzing the glycosylation state of the IFN-β produced. Human IFN-β, in contrast to multiple subspecies of IFN-α, is a glycoprotein with a single potential N-linked carbohydrate attachment signal located at residues 80–82. The physical properties and specific activity of E. coli IFN-β differ significantly from those of its natural counterpart. Indirect methods with tunicamycin or other metabolic inhibitors of glycosylation suggest that some biologically active, unglycosylated IFN-β is produced and secreted into the media in the presence of such inhibitors. Glycoproteins are known to bind to concanavalin A (con A) and can therefore be separated from nonglycosylated proteins by chromatography on Con A-sepharose. The 18,500 D form of IFN-β produced from the pMB-1 gene appears to be unglycosylated confirming that the asparagine residue at position 80 is the site for glycosylation in native IFN-β. Preliminary results indicate that the unglycosylated IFN-β produced and secreted from the mutant gene has a much lower specific biological activity than glycosylated IFN-β. The availability of these cell lines permits to evaluate further the role of glycosylation in the activity and physical properties of IFN-β." @default.
- W1233964385 created "2016-06-24" @default.
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- W1233964385 date "1986-01-01" @default.
- W1233964385 modified "2023-09-25" @default.
- W1233964385 title "[57] Procedures for expression, modification, and analysis of human fibroblast interferon (IFN-β) genes in heterologous cells" @default.
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- W1233964385 doi "https://doi.org/10.1016/0076-6879(86)19059-8" @default.
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