Two Molecular Species of Mouse L Cell Interferon Differing in Lectin Binding

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Abstract
Binding of [mouse fibroblast] L cell interferon to lectins, Wistaria floribunda agglutinin (WFA) and concanavalin A (Con A) was studied by affinity chromatography. Of the 2 molecular species of L cell interferon F (MW 24,000) and S (MW 36,000) only the latter was bound efficiently to WFA-Sepharose and eluted quantitatively with D-galactose followed by a pH 3 buffer, suggesting a substantial difference between the 2 interferon species in their carbohydrate structure. Both were partially bound to Con A-Sepharose and eluted with .alpha.-methyl-D-glucoside; apparently at least some of the F species are also glycoprotein and both F and S interferons are heterogeneous in their affinity to this lectin.