作者: T Arakawa , N K Alton , Y R Hsu
DOI: 10.1016/S0021-9258(17)38587-3
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摘要: An attempt was made to prepare a highly purified, active recombinant DNA-derived human interferon-gamma. When the protein denatured in urea and refolded, gel filtration sedimentation velocity experiments indicated presence of two forms, which are different size not rapid reversible equilibrium. The forms could be chromatographically separated. Far-UV circular dichroic spectra secondary structures for both forms. Near-UV revealed that smaller form is folded into rigid tertiary structure. antiviral activity interferon-gamma showed significant difference, i.e. 4-8-fold more than larger form. A variety show active, homogeneous, soluble, stable