1986 年 99 巻 5 号 p. 1533-1535
The conformations of fibroblast and E. coli-derived recombinant human interferon-βs were studied by circular dichroism and nuclear magnetic resonance spectroscopy in the acidic pH region of 4.6 to 1.6. Both interferons have very similar conformations with high α-helix contents (_??_70%). These results suggest that glycosylation does not appreciably change the conformation of human interferon-β. Moreover, a slow conformational change is observed below pH 2.0, which induces the disruption of β-sheets.