Altered molecular species of human interferon produced in the presence of inhibitors of glycosylation.

The inhibitors of glycosylation, 2-deoxy-D-glucose or D-glucosamine, inhibit the synthesis of biologically active interferon in human FS-4 fibroblast cultures stimulated with polyinosinate-polycytidylate. Interferon synthesized in the presence of partially inhibitory concentrations of 2-deoxy-D-glucose or D-glucosamine were found to differ from interferons made in control cultures in some physical properties. Interferons synthesized in the presence of either inhibitor had a diminished charge heterogeneity demonstrable by iso-electric focusing. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, control interferon activity formed a single peak with the apparent molecular weight of 20,000, whereas interferons from cultures treated with either inhibitor could be resolved into two distinct molecular weight components, one of which was smaller than the interferon synthesized in control cultures.