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- W2008760839 abstract "Human interferon-ß1 is extremely stable in a low ionic strength solution of pH 2 such as 10 mM HCl at 37°C. However, the presence of 0.15 M NaCl led to a remarkable loss of antiviral activity. The molecular-sieve high-performance liquid chromatography revealed that, whereas completely active human interferon-ß1 eluted as a 25 kDa species (monomeric form), the inactivated preparation eluted primarily as a 90 kDa species (oligomeric form). The specific activity (units per protein) of the oligomeric form was approx. 10% of that of the monomeric form. This observation shows that oligomeric human interferon-ß1 is apparently in an inactive form. When the oligomeric eluate was resolved by polyacrylamide gel containing sodium dodecyl sulphate (SDS), it appeared to be monomeric under non-reducing conditions. Monomerization of the oligomeric human interferon-ß1 by treatment with 1% SDS, fully regenerated its antiviral activity. These results suggest that the inactivation of the human interferon-ß1 preparation was caused by its oligomerization via hydrophobic interactions without the formation of intermolecular disulphide bonds. These oligomers can be dissociated by SDS to restore biological activity." @default.
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- W2008760839 date "1989-10-01" @default.
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- W2008760839 title "Stability of human interferon-ß1: oligomeric human interferon-ß1 is inactive but is reactivated by monomerization" @default.
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- W2008760839 doi "https://doi.org/10.1016/0167-4838(89)90269-0" @default.
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