Oligomeric structure of recombinant human and murine immune interferons by means of sedimentation equilibrium.
The oligomeric structure of two recombinant human immune interferon species, one with Cys-Tyr-Cys-Gln [( Cys-Tyr-Cys]rHu-IFN-gamma) and the other with Met-Gln-Asp-Pro (rHu-IFN-gamma) as the amino-terminal residues, and a recombinant murine immune interferon [( Cys-Tyr-Cys]rMu-IFN-gamma) were examined by means of sedimentation equilibrium. All three IFN-gamma s existed as dimers under nondenaturing conditions. Both [Cys-Tyr-Cys]rHu-IFN-gamma and [Cys-Tyr-Cys]rMu-IFN-gamma formed higher oligomers, tetramers, and octamers, respectively, under oxidative conditions, whereas rHu-IFN-gamma remained as dimers.
D000818:Animals; D000975:Antioxidants; D006801:Humans; D007371:Interferon-gamma / Q000302:isolation & purification; D051379:Mice; D008970:Molecular Weight; D011487:Protein Conformation; D011489:Protein Denaturation; D014461:Ultracentrifugation
D000975:Antioxidants; D007371:Interferon-gamma