Characterization of four different mammalian‐cell‐derived recombinant human interferon‐β1s

摘要: In order to evaluate the structural identification of various recombinant human interferon-β1s, proteins were produced in four different mammalian cells (human PC12 and PC8 lung adenocarcinoma cells, Chinese hamster ovary mouse C127 cells) characterized. Each mammalian-cell-derived interferon-β1 represented a single band 23 kDa on sodium dodecyl sulphate/polyacrylamide gel electrophoresis, same molecular mass as fibroblast-derived natural interferon-β1. Specific activities, amino acid compositions, amino-terminal sequences, peptide maps C18 reversed-phase high-performance liquid chromatography circular dichroic spectra good agreement with ones. On other hand, patterns isoelectric focusing between interferon-β1s Sugar composition analysis revealed that protein from has similar sugar have increased amounts galactose glucosamine comparison protein. Furthermore, there is no galactosamine protein, while small detected oligosaccharides released PC8- C127-derived by N-glycanase. These results indicate identical polypeptides those but their carbohydrate moieties, including unusual N-linked oligosaccharides, are individually ones depend host cell.