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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.
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.