1887

Abstract

Summary

Altering the aqueous environment, especially with agents that affect hydrogen bonds, markedly affects the stability of mouse L cell interferon. Low pH stabilizes interferon whereas high pH labilizes it; heavy water further enhances interferon thermostability at pH 2 but not at pH 9. Exposure to the protein denaturants, 4 -guanidine hydrochloride and 6 -urea, significantly decreases the activity of interferon at pH 2 and pH 9; however, the residual interferon activity is relatively thermostable. Certain chaotropic salts protect interferon against thermal destruction, and in terms of effectiveness, their sequence is in the order SCN > I ⩾ Cl = ClO = Br > NO . Interferon becomes more stable to heat as the NaSCN concentration is increased from 0.25 to 2.0 . Molecular sieve chromatography of interferon in the presence of 1.5 -NaSCN at pH 7 shows a shift in its apparent mol. wt. from 25000 to 42000. Unlike most proteins, the unfolded conformation of interferon appears to be more stable to heat than the molecule with a smaller Stokes' radius.

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/content/journal/jgv/10.1099/0022-1317-35-1-45
1977-04-01
2019-10-23
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-35-1-45
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