Binding of L cell interferon to lectins, agglutinin (WFA) and concanavalin A (Con A) was studied by affinity chromatography. Of the two molecular species of L cell interferon, F (mol. wt. 24000) and S (mol. wt. 36000), only the latter was bound efficiently to WFA-Sepharose and eluted quantitatively with -galactose followed by a pH 3 buffer, suggesting a substantial difference between the two interferon species in their carbohydrate structure. Both were partially bound to Con A-Sepharose and eluted with α-methyl--glucoside, indicating that at least some of the F species are also glycoprotein, and that both F and S interferons are heterogeneous as regards their affinity to this lectin.


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